Flavin adenine dinucleotide

Identification

Summary

Flavin adenine dinucleotide is a coenzyme form of vitamin B2 used in clinical conditions associated with vitamin B2 deficiency.

Brand Names
EnBrace HR, EnLyte
Generic Name
Flavin adenine dinucleotide
DrugBank Accession Number
DB03147
Background

A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972) Flavin adenine dinucleotide is approved for use in Japan under the trade name Adeflavin as an ophthalmic treatment for vitamin B2 deficiency.

Type
Small Molecule
Groups
Approved
Structure
Weight
Average: 785.5497
Monoisotopic: 785.157134455
Chemical Formula
C27H33N9O15P2
Synonyms
  • Adenosine 5'-(trihydrogen pyrophosphate), 5'-5'-ester with riboflavine
  • adenosine 5'-[3-(riboflavin-5'-yl) dihydrogen diphosphate]
  • FAD
  • Flavin adenine dinucleotide
  • Flavin-Adenine Dinucleotide
  • Flavine adenine dinucleotide
  • Riboflavin 5'-(trihydrogen diphosphate), 5'-5'-ester with adenosine
  • Riboflavin 5'-adenosine diphosphate

Pharmacology

Indication

Used to treat eye diseases caused by vitamin B2 deficiency, such as keratitis and blepharitis.

Reduce drug development failure rates
Build, train, & validate machine-learning models
with evidence-based and structured datasets.
See how
Build, train, & validate predictive machine-learning models with structured datasets.
See how
Associated Therapies
Contraindications & Blackbox Warnings
Prevent Adverse Drug Events Today
Tap into our Clinical API for life-saving information on contraindications & blackbox warnings, population restrictions, harmful risks, & more.
Learn more
Avoid life-threatening adverse drug events with our Clinical API
Learn more
Pharmacodynamics

Not Available

Mechanism of action
TargetActionsOrganism
ARibosyldihydronicotinamide dehydrogenase [quinone]
inhibitor
Humans
ANitric oxide synthase 1
inhibitor
Humans
ADihydropyrimidine dehydrogenase [NADP(+)]
inhibitor
Humans
AXanthine dehydrogenase/oxidase
inhibitor
Humans
AGlutathione reductase, mitochondrial
inhibitor
Humans
ANAD(P)H dehydrogenase [quinone] 1
inhibitor
Humans
AAmine oxidase [flavin-containing] A
inhibitor
Humans
AThioredoxin reductase 1, cytoplasmic
inhibitor
Humans
AAmine oxidase [flavin-containing] B
inhibitor
Humans
UNADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
cofactor
Humans
Up-hydroxybenzoate hydroxylaseNot AvailablePseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Up-hydroxybenzoate hydroxylaseNot AvailablePseudomonas fluorescens
UFumarate reductase flavoprotein subunitNot AvailableShewanella oneidensis (strain MR-1)
UERO1-like protein betaNot AvailableHumans
UNADPH-ferredoxin reductase FprANot AvailableMycobacterium tuberculosis
UNADH-cytochrome b5 reductase 3Not AvailableHumans
UCholesterol oxidaseNot AvailableStreptomyces sp. (strain SA-COO)
UThymidylate synthase ThyXNot AvailableThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
UPyruvate oxidaseNot AvailableLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
UGlutathione reductaseNot AvailableEscherichia coli (strain K12)
UMonomeric sarcosine oxidaseNot AvailableBacillus sp. (strain B-0618)
UTrypanothione reductaseNot AvailableTrypanosoma cruzi
UIsovaleryl-CoA dehydrogenase, mitochondrialNot AvailableHumans
UCholesterol oxidaseNot AvailableBrevibacterium sterolicum
UD-lactate dehydrogenaseNot AvailableEscherichia coli (strain K12)
UIsobutyryl-CoA dehydrogenase, mitochondrialNot AvailableHumans
UApoptosis-inducing factor 1, mitochondrialNot AvailableHumans
UUDP-galactopyranose mutaseNot AvailableEscherichia coli (strain K12)
UFlavohemoproteinNot AvailableCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
UGlycine oxidaseNot AvailableBacillus subtilis (strain 168)
UNADPH--cytochrome P450 reductaseNot AvailableHumans
UGlutaryl-CoA dehydrogenase, mitochondrialNot AvailableHumans
UMedium-chain specific acyl-CoA dehydrogenase, mitochondrialNot AvailableHumans
UD-amino-acid oxidaseNot AvailableHumans
UBifunctional protein PutANot AvailableEscherichia coli (strain K12)
UDeoxyribodipyrimidine photo-lyaseNot AvailableThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
UShort-chain specific acyl-CoA dehydrogenase, mitochondrialNot AvailableHumans
UL-amino-acid oxidaseNot AvailableHumans
U2,4-dienoyl-CoA reductase [NADPH]Not AvailableEscherichia coli (strain K12)
U2-oxopropyl-CoM reductase, carboxylatingNot AvailableXanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
UFumarate reductase flavoprotein subunitNot AvailableShewanella frigidimarina
UThioredoxin reductaseNot AvailableEscherichia coli (strain K12)
U5,10-methylenetetrahydrofolate reductaseNot AvailableEscherichia coli (strain K12)
UDimethylglycine oxidaseNot AvailableArthrobacter globiformis
UNADH peroxidaseNot AvailableEnterococcus faecalis (strain ATCC 700802 / V583)
UFerredoxin--NADP reductaseNot AvailableAnabaena sp. (strain PCC 7119)
USulfite reductase [NADPH] flavoprotein alpha-componentNot AvailableEscherichia coli (strain K12)
UFerredoxin--NADP reductaseNot AvailableAzotobacter vinelandii
UAcyl-CoA dehydrogenase, short-chain specificNot AvailableMegasphaera elsdenii
UFerredoxin reductaseNot AvailablePseudomonas sp. (strain KKS102)
UDihydrolipoyl dehydrogenaseNot AvailableAzotobacter vinelandii
UAmine oxidase, flavin-containing proteinNot AvailablePseudomonas syringae pv. tomato (strain DC3000)
UDeoxyribodipyrimidine photo-lyaseNot AvailableEscherichia coli (strain K12)
UDeoxyribodipyrimidine photo-lyaseNot AvailableSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
UL-aspartate oxidaseNot AvailableEscherichia coli (strain K12)
UCryptochrome DASHNot AvailableSynechocystis sp. (strain PCC 6803 / Kazusa)
UDihydrolipoyl dehydrogenase, mitochondrialNot AvailableHumans
UFumarate reductase flavoprotein subunitNot AvailableShewanella frigidimarina (strain NCIMB 400)
UNADH-cytochrome b5 reductase 1Not AvailableHumans
UOxidoreductaseNot AvailableBrevibacterium sterolicum
UNADPH:adrenodoxin oxidoreductase, mitochondrialNot AvailableHumans
UPeroxisomal acyl-coenzyme A oxidase 1Not AvailableHumans
UUDP-N-acetylenolpyruvoylglucosamine reductaseNot AvailableEscherichia coli (strain K12)
UFAD-linked sulfhydryl oxidase ALRNot AvailableHumans
UUDP-N-acetylenolpyruvoylglucosamine reductaseNot AvailableStaphylococcus aureus (strain MW2)
UFlavohemoproteinNot AvailableEscherichia coli (strain K12)
UPhenol 2-hydroxylase component BNot AvailableBacillus thermoglucosidasius
UMethylenetetrahydrofolate reductaseNot AvailableThermus thermophilus
UPutidaredoxin reductaseNot AvailablePseudomonas putida
UNAD(P)H dehydrogenase (quinone)Not AvailableMycobacterium tuberculosis
UUDP-galactopyranose mutaseNot AvailableMycobacterium tuberculosis
U4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA-Delta-isomeraseNot AvailableClostridium aminobutyricum
U4-cresol dehydrogenase [hydroxylating] flavoprotein subunitNot AvailablePseudomonas putida
UAlkyl hydroperoxide reductase subunit FNot AvailableSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
UDihydrolipoyl dehydrogenaseNot AvailableNeisseria meningitidis
UGlutathione reductaseNot AvailablePlasmodium falciparum (isolate K1 / Thailand)
UPhenylacetone monooxygenaseNot AvailableThermobifida fusca (strain YX)
UBenzoate 1,2-dioxygenase electron transfer componentNot AvailableAcinetobacter sp. (strain ADP1)
UPutative acyl-CoA dehydrogenaseNot AvailableThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
UFkbINot AvailableStreptomyces hygroscopicus subsp. ascomyceticus
UDihydrolipoyl dehydrogenaseNot AvailablePseudomonas putida
UDihydrolipoyl dehydrogenaseNot AvailablePseudomonas fluorescens
UAlkyl hydroperoxide reductase subunit FNot AvailableEscherichia coli (strain K12)
UFerredoxin--NADP reductaseNot AvailableNostoc sp. (strain PCC 7120 / UTEX 2576)
UFerredoxin--NADP reductaseNot AvailableEscherichia coli (strain K12)
UMersacidin decarboxylaseNot AvailableBacillus sp. (strain HIL-Y85/54728)
Absorption

Not Available

Volume of distribution

Not Available

Protein binding

Not Available

Metabolism
Not Available
Route of elimination

Not Available

Half-life

Not Available

Clearance

Not Available

Adverse Effects
Improve decision support & research outcomes
With structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!
See the data
Improve decision support & research outcomes with our structured adverse effects data.
See a data sample
Toxicity

Oral mouse LD50 > 7000 mg/kg. Intravenous mouse LD50 589 mg/kg.

Pathways
PathwayCategory
Glutathione MetabolismMetabolic
Caffeine MetabolismMetabolic
Valine, Leucine, and Isoleucine DegradationMetabolic
Lysine DegradationMetabolic
Folate MetabolismMetabolic
Tryptophan MetabolismMetabolic
Riboflavin MetabolismMetabolic
Lovastatin Action PathwayDrug action
Cerivastatin Action PathwayDrug action
Glycerol Phosphate ShuttleMetabolic
3-Methylglutaconic Aciduria Type IIIDisease
3-Methylglutaconic Aciduria Type IVDisease
5-OxoprolinuriaDisease
Adenylosuccinate Lyase DeficiencyDisease
Dihydropyrimidine Dehydrogenase Deficiency (DHPD)Disease
Ethylmalonic EncephalopathyDisease
Glutaric Aciduria Type IDisease
Glycerol Kinase DeficiencyDisease
Maple Syrup Urine DiseaseDisease
Methylmalonic Aciduria Due to Cobalamin-Related DisordersDisease
PhenylketonuriaDisease
HypercholesterolemiaDisease
S-Adenosylhomocysteine (SAH) Hydrolase DeficiencyDisease
Xanthine Dehydrogenase Deficiency (Xanthinuria)Disease
Glycine N-Methyltransferase DeficiencyDisease
Short-Chain Acyl-CoA Dehydrogenase Deficiency (SCAD Deficiency)Disease
Propionic AcidemiaDisease
3-Methylcrotonyl-CoA Carboxylase Deficiency Type IDisease
Isovaleric AciduriaDisease
Dimethylglycine Dehydrogenase DeficiencyDisease
Pharmacogenomic Effects/ADRs
Not Available

Interactions

Drug Interactions
This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.
Not Available
Food Interactions
  • Avoid alcohol. Ingesting alcohol may reduce the absorption of FAD.

Products

Drug product information from 10+ global regions
Our datasets provide approved product information including:
dosage, form, labeller, route of administration, and marketing period.
Access now
Access drug product information from over 10 global regions.
Access now
Product Ingredients
IngredientUNIICASInChI Key
Flavin adenine dinucleotide disodium67U7UHJ04C84366-81-4XLRHXNIVIZZOON-WFUPGROFSA-N
International/Other Brands
Adeflavin / Flaziren
Mixture Products
NameIngredientsDosageRouteLabellerMarketing StartMarketing EndRegionImage
PramLyteFlavin adenine dinucleotide (25 ug/1) + 1,2-docosahexanoyl-sn-glycero-3-phosphoserine calcium (6.4 mg/1) + 1,2-icosapentoyl-sn-glycero-3-phosphoserine calcium (800 ug/1) + Betaine (500 ug/1) + Citric acid monohydrate (1.83 mg/1) + Cobamamide (50 ug/1) + Cocarboxylase (25 ug/1) + Escitalopram oxalate (10 mg/1) + Ferrous cysteine glycinate (13.6 mg/1) + Folic acid (1 mg/1) + Leucovorin (2.5 mg/1) + Levomefolate magnesium (7 mg/1) + Magnesium ascorbate (24 mg/1) + NADH (25 ug/1) + Phosphatidyl serine (12 mg/1) + Pyridoxal phosphate (25 ug/1) + Sodium citrate (3.67 mg/1) + Zinc ascorbate (1 mg/1)KitOralAllegis Pharmaceuticals, LLC2015-09-112016-01-04US flag
Unapproved/Other Products
NameIngredientsDosageRouteLabellerMarketing StartMarketing EndRegionImage
BumP DHAFlavin adenine dinucleotide (1 mg/1) + Cobamamide (500 mg/1) + Flavin mononucleotide (2 mg/1) + Iron (15 mg/1) + Leucovorin (1 mg/1) + Levomefolate magnesium (1 mg/1) + Magnesium oxide (125 mg/1) + NADH (25 ug/1) + Omega-3 fatty acids (300 mg/1) + Potassium Iodide (250 ug/1) + Pyridoxal phosphate (5 mg/1) + Pyridoxine hydrochloride (20 mg/1) + Zinc glycinate (15 1/1)CapsuleOralCenturion Labs2017-03-242017-04-17US flag
EnBrace HRFlavin adenine dinucleotide (25 ug/1) + 1,2-docosahexanoyl-sn-glycero-3-phosphoserine calcium (6.4 mg/1) + 1,2-icosapentoyl-sn-glycero-3-phosphoserine calcium (800 ug/1) + Betaine (500 ug/1) + Cobamamide (50 ug/1) + Cocarboxylase (25 ug/1) + Ferrous cysteine glycinate (13.6 mg/1) + Folic acid (1 mg/1) + Magnesium L-threonate (1 mg/1) + Leucovorin (2.5 mg/1) + Levomefolate magnesium (5.23 mg/1) + Magnesium ascorbate (24 mg/1) + NADH (25 ug/1) + Phosphatidyl serine (12 mg/1) + Pyridoxal phosphate (25 ug/1) + Zinc ascorbate (1 mg/1)Capsule, delayed release pelletsOralJaymac Pharma2011-08-12Not applicableUS flag
PaxLyteFlavin adenine dinucleotide (025 ug/1) + 1,2-docosahexanoyl-sn-glycero-3-phosphoserine calcium (6.4 mg/1) + 1,2-icosapentoyl-sn-glycero-3-phosphoserine calcium (800 ug/1) + Betaine (500 mg/1) + Citric acid monohydrate (1.83 mg/1) + Cobamamide (50 ug/1) + Cocarboxylase (25 ug/1) + Ferrous cysteine glycinate (13.6 mg/1) + Folic acid (1 mg/1) + Magnesium L-threonate (1 mg/1) + Leucovorin (2.5 mg/1) + Levomefolate magnesium (7 mg/1) + Magnesium ascorbate (24 mg/1) + NADH (25 ug/1) + Phosphatidyl serine (12 mg/1) + Pyridoxal phosphate (25 ug/1) + Sodium citrate (1.83 mg/1) + Zinc ascorbate (1 mg/1)CapsuleOralJayMac Pharmaceuticals2024-08-01Not applicableUS flag

Categories

Drug Categories
Chemical TaxonomyProvided by Classyfire
Description
This compound belongs to the class of organic compounds known as flavin nucleotides. These are nucleotides containing a flavin moiety. Flavin is a compound that contains the tricyclic isoalloxazine ring system, which bears 2 oxo groups at the 2- and 4-positions.
Kingdom
Organic compounds
Super Class
Nucleosides, nucleotides, and analogues
Class
Flavin nucleotides
Sub Class
Not Available
Direct Parent
Flavin nucleotides
Alternative Parents
(3'->5')-dinucleotides / Purine ribonucleoside diphosphates / Purine ribonucleoside monophosphates / Flavins / Pentose phosphates / Glycosylamines / 6-aminopurines / Quinoxalines / Monosaccharide phosphates / Organic pyrophosphates
show 19 more
Substituents
(3'->5')-dinucleotide / (3'->5')-dinucleotide or analogue / 6-aminopurine / Alcohol / Alkyl phosphate / Amine / Aminopyrimidine / Aromatic heteropolycyclic compound / Azacycle / Azole
show 44 more
Molecular Framework
Aromatic heteropolycyclic compounds
External Descriptors
flavin adenine dinucleotide (CHEBI:16238)
Affected organisms
  • Humans and other mammals

Chemical Identifiers

UNII
ZC44YTI8KK
CAS number
146-14-5
InChI Key
VWWQXMAJTJZDQX-UYBVJOGSSA-N
InChI
InChI=1S/C27H33N9O15P2/c1-10-3-12-13(4-11(10)2)35(24-18(32-12)25(42)34-27(43)33-24)5-14(37)19(39)15(38)6-48-52(44,45)51-53(46,47)49-7-16-20(40)21(41)26(50-16)36-9-31-17-22(28)29-8-30-23(17)36/h3-4,8-9,14-16,19-21,26,37-41H,5-7H2,1-2H3,(H,44,45)(H,46,47)(H2,28,29,30)(H,34,42,43)/t14-,15+,16+,19-,20+,21+,26+/m0/s1
IUPAC Name
{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}[({[(2R,3S,4S)-5-{7,8-dimethyl-2,4-dioxo-2H,3H,4H,10H-benzo[g]pteridin-10-yl}-2,3,4-trihydroxypentyl]oxy}(hydroxy)phosphoryl)oxy]phosphinic acid
SMILES
CC1=CC2=C(C=C1C)N(C[C@H](O)[C@H](O)[C@H](O)CO[P@](O)(=O)O[P@@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC3=C1N=CN=C3N)C1=NC(=O)NC(=O)C1=N2

References

General References
Not Available
Human Metabolome Database
HMDB0001248
KEGG Drug
D00005
KEGG Compound
C00016
PubChem Compound
643975
PubChem Substance
46508543
ChemSpider
559059
RxNav
1314412
ChEBI
16238
ChEMBL
CHEMBL1232653
ZINC
ZINC000008215434
PDBe Ligand
FAD
Wikipedia
Flavin_adenine_dinucleotide
PDB Entries
1a8p / 1ahv / 1ahz / 1amo / 1an9 / 1aog / 1b2r / 1b37 / 1b4v / 1b5q …
show 2875 more
MSDS
Download (692 KB)

Clinical Trials

Clinical Trials
Clinical Trial & Rare Diseases Add-on Data Package
Explore 4,000+ rare diseases, orphan drugs & condition pairs, clinical trial why stopped data, & more. Preview package
PhaseStatusPurposeConditionsCountStart DateWhy Stopped100+ additional columns
4WithdrawnTreatmentMenstrual Related Mood Disorder / Premenstrual Dysphoric Disorder (PMDD) / Premenstrual Syndrome (PMS) / Premenstrual tension with edema1somestatusstop reasonjust information to hide

Pharmacoeconomics

Manufacturers
Not Available
Packagers
Not Available
Dosage Forms
FormRouteStrength
CapsuleOral
Capsule, liquid filledOral
Capsule, delayed release pelletsOral
KitOral
Prices
Not Available
Patents
Not Available

Properties

State
Solid
Experimental Properties
Not Available
Predicted Properties
PropertyValueSource
Water Solubility4.25 mg/mLALOGPS
logP-0.78ALOGPS
logP-4.8Chemaxon
logS-2.3ALOGPS
pKa (Strongest Acidic)1.85Chemaxon
pKa (Strongest Basic)4.89Chemaxon
Physiological Charge-3Chemaxon
Hydrogen Acceptor Count19Chemaxon
Hydrogen Donor Count9Chemaxon
Polar Surface Area356.42 Ã…2Chemaxon
Rotatable Bond Count13Chemaxon
Refractivity177.43 m3·mol-1Chemaxon
Polarizability70.53 Ã…3Chemaxon
Number of Rings6Chemaxon
Bioavailability0Chemaxon
Rule of FiveNoChemaxon
Ghose FilterNoChemaxon
Veber's RuleNoChemaxon
MDDR-like RuleYesChemaxon
Predicted ADMET Features
PropertyValueProbability
Human Intestinal Absorption-0.6156
Blood Brain Barrier+0.5
Caco-2 permeable-0.6995
P-glycoprotein substrateSubstrate0.6464
P-glycoprotein inhibitor INon-inhibitor0.7931
P-glycoprotein inhibitor IINon-inhibitor0.9705
Renal organic cation transporterNon-inhibitor0.9561
CYP450 2C9 substrateNon-substrate0.8093
CYP450 2D6 substrateNon-substrate0.8312
CYP450 3A4 substrateSubstrate0.5632
CYP450 1A2 substrateNon-inhibitor0.8426
CYP450 2C9 inhibitorNon-inhibitor0.8818
CYP450 2D6 inhibitorNon-inhibitor0.8636
CYP450 2C19 inhibitorNon-inhibitor0.872
CYP450 3A4 inhibitorNon-inhibitor0.7323
CYP450 inhibitory promiscuityLow CYP Inhibitory Promiscuity0.8967
Ames testNon AMES toxic0.8242
CarcinogenicityNon-carcinogens0.8105
BiodegradationNot ready biodegradable0.9965
Rat acute toxicity2.5009 LD50, mol/kg Not applicable
hERG inhibition (predictor I)Weak inhibitor0.9501
hERG inhibition (predictor II)Inhibitor0.578
ADMET data is predicted using admetSAR, a free tool for evaluating chemical ADMET properties. (23092397)

Spectra

Mass Spec (NIST)
Not Available
Spectra
SpectrumSpectrum TypeSplash Key
Predicted GC-MS Spectrum - GC-MSPredicted GC-MSsplash10-0170-1032960400-cdd3286ebb1dea7c4f54
MS/MS Spectrum - Quattro_QQQ 10V, PositiveLC-MS/MSsplash10-000i-0001200900-b0740b3d33d50996ccde
MS/MS Spectrum - Quattro_QQQ 25V, PositiveLC-MS/MSsplash10-000m-0105900000-3abff26d5bb35f8527b8
MS/MS Spectrum - Quattro_QQQ 40V, PositiveLC-MS/MSsplash10-000i-0931700000-73f360589a13230eea7a
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-000j-0908600300-b1eccda8ebae8b9e4cc1
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-000i-0900000000-bdb826f9c3cbc09eff9b
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-00di-0019800000-00ad56b6b6a3bb4516e6
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-000b-0009400000-667064ca470a5c341974
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-000j-0509700500-8766cb874f927ed5a795
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-000i-0900000000-3125e04c09a14c62f22a
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-00di-0019700000-78c46ea4b4f562757e56
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-000b-0009400000-94b845d2c8d082b9484c
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-001i-0000100900-6bac7b7f631dfc074a0c
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-001i-0920000000-49c9d4fb9b57a59f45a5
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-000i-0003900000-572f0b1bd59f71ab3c5f
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-000i-0003900000-d2ede6a2e7183f1c32a3
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-001i-0000100900-78554afbc26abe26af35
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-001i-0930000000-274da0a01c651b791733
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-000i-0003900000-55939cda9e14fc582757
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , NegativeLC-MS/MSsplash10-000i-0003900000-db784762434fac3d351f
Predicted MS/MS Spectrum - 10V, Positive (Annotated)Predicted LC-MS/MSsplash10-000i-0002000900-0a9583645f34f571fbd6
Predicted MS/MS Spectrum - 10V, Negative (Annotated)Predicted LC-MS/MSsplash10-00lr-0000000900-8683c1d1c2f4739118fd
Predicted MS/MS Spectrum - 20V, Positive (Annotated)Predicted LC-MS/MSsplash10-0frj-0277120900-81692b59b61e9511a547
Predicted MS/MS Spectrum - 20V, Negative (Annotated)Predicted LC-MS/MSsplash10-015c-2101231900-93249ce945a5aa44dfa2
Predicted MS/MS Spectrum - 40V, Positive (Annotated)Predicted LC-MS/MSsplash10-000i-0596100300-a65e069aefb170b3864d
Predicted MS/MS Spectrum - 40V, Negative (Annotated)Predicted LC-MS/MSsplash10-00l2-8610531900-1df93c013e1605e4cc93
1H NMR Spectrum1D NMRNot Applicable
[1H,1H] 2D NMR Spectrum2D NMRNot Applicable
[1H,13C] 2D NMR Spectrum2D NMRNot Applicable
Chromatographic Properties
Collision Cross Sections (CCS)
AdductCCS Value (â„«2)Source typeSource
[M-H]-277.5674337
predicted
DarkChem Lite v0.1.0
[M-H]-273.0312337
predicted
DarkChem Lite v0.1.0
[M-H]-293.8611337
predicted
DarkChem Lite v0.1.0
[M-H]-243.13689
predicted
DeepCCS 1.0 (2019)
[M+H]+277.4043337
predicted
DarkChem Lite v0.1.0
[M+H]+273.2360337
predicted
DarkChem Lite v0.1.0
[M+H]+244.86061
predicted
DeepCCS 1.0 (2019)
[M+Na]+275.9832337
predicted
DarkChem Lite v0.1.0
[M+Na]+272.8946337
predicted
DarkChem Lite v0.1.0
[M+Na]+251.18956
predicted
DeepCCS 1.0 (2019)

Targets

Build, predict & validate machine-learning models
Use our structured and evidence-based datasets to unlock new
insights and accelerate drug research.
Learn more
Use our structured and evidence-based datasets to unlock new insights and accelerate drug research.
Learn more
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Inhibitor
General Function
The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis
Specific Function
Chloride ion binding
Gene Name
NQO2
Uniprot ID
P16083
Uniprot Name
Ribosyldihydronicotinamide dehydrogenase [quinone]
Molecular Weight
25918.4 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Zhou Y, Zhang Y, Zhao D, Yu X, Shen X, Zhou Y, Wang S, Qiu Y, Chen Y, Zhu F: TTD: Therapeutic Target Database describing target druggability information. Nucleic Acids Res. 2024 Jan 5;52(D1):D1465-D1477. doi: 10.1093/nar/gkad751. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Inhibitor
General Function
Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR
Specific Function
Arginine binding
Gene Name
NOS1
Uniprot ID
P29475
Uniprot Name
Nitric oxide synthase 1
Molecular Weight
160969.095 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
  4. Zhou Y, Zhang Y, Zhao D, Yu X, Shen X, Zhou Y, Wang S, Qiu Y, Chen Y, Zhu F: TTD: Therapeutic Target Database describing target druggability information. Nucleic Acids Res. 2024 Jan 5;52(D1):D1465-D1477. doi: 10.1093/nar/gkad751. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Inhibitor
General Function
Involved in pyrimidine base degradation (PubMed:1512248). Catalyzes the reduction of uracil and thymine (PubMed:1512248). Also involved the degradation of the chemotherapeutic drug 5-fluorouracil (PubMed:1512248)
Specific Function
4 iron, 4 sulfur cluster binding
Gene Name
DPYD
Uniprot ID
Q12882
Uniprot Name
Dihydropyrimidine dehydrogenase [NADP(+)]
Molecular Weight
111400.32 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
  4. Zhou Y, Zhang Y, Zhao D, Yu X, Shen X, Zhou Y, Wang S, Qiu Y, Chen Y, Zhu F: TTD: Therapeutic Target Database describing target druggability information. Nucleic Acids Res. 2024 Jan 5;52(D1):D1465-D1477. doi: 10.1093/nar/gkad751. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Inhibitor
General Function
Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro)
Specific Function
2 iron, 2 sulfur cluster binding
Gene Name
XDH
Uniprot ID
P47989
Uniprot Name
Xanthine dehydrogenase/oxidase
Molecular Weight
146422.99 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
  4. Zhou Y, Zhang Y, Zhao D, Yu X, Shen X, Zhou Y, Wang S, Qiu Y, Chen Y, Zhu F: TTD: Therapeutic Target Database describing target druggability information. Nucleic Acids Res. 2024 Jan 5;52(D1):D1465-D1477. doi: 10.1093/nar/gkad751. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Inhibitor
General Function
Maintains high levels of reduced glutathione in the cytosol
Specific Function
Electron transfer activity
Gene Name
GSR
Uniprot ID
P00390
Uniprot Name
Glutathione reductase, mitochondrial
Molecular Weight
56256.565 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Zhou Y, Zhang Y, Zhao D, Yu X, Shen X, Zhou Y, Wang S, Qiu Y, Chen Y, Zhu F: TTD: Therapeutic Target Database describing target druggability information. Nucleic Acids Res. 2024 Jan 5;52(D1):D1465-D1477. doi: 10.1093/nar/gkad751. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Inhibitor
General Function
Flavin-containing quinone reductase that catalyzes two-electron reduction of quinones to hydroquinones using either NADH or NADPH as electron donors. In a ping-pong kinetic mechanism, the electrons are sequentially transferred from NAD(P)H to flavin cofactor and then from reduced flavin to the quinone, bypassing the formation of semiquinone and reactive oxygen species (By similarity) (PubMed:8999809, PubMed:9271353). Regulates cellular redox state primarily through quinone detoxification. Reduces components of plasma membrane redox system such as coenzyme Q and vitamin quinones, producing antioxidant hydroquinone forms. In the process may function as superoxide scavenger to prevent hydroquinone oxidation and facilitate excretion (PubMed:15102952, PubMed:8999809, PubMed:9271353). Alternatively, can activate quinones and their derivatives by generating redox reactive hydroquinones with DNA cross-linking antitumor potential (PubMed:8999809). Acts as a gatekeeper of the core 20S proteasome known to degrade proteins with unstructured regions. Upon oxidative stress, interacts with tumor suppressors TP53 and TP73 in a NADH-dependent way and inhibits their ubiquitin-independent degradation by the 20S proteasome (PubMed:15687255, PubMed:28291250)
Specific Function
Cytochrome-b5 reductase activity, acting on nad(p)h
Gene Name
NQO1
Uniprot ID
P15559
Uniprot Name
NAD(P)H dehydrogenase [quinone] 1
Molecular Weight
30867.405 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
  4. Zhou Y, Zhang Y, Zhao D, Yu X, Shen X, Zhou Y, Wang S, Qiu Y, Chen Y, Zhu F: TTD: Therapeutic Target Database describing target druggability information. Nucleic Acids Res. 2024 Jan 5;52(D1):D1465-D1477. doi: 10.1093/nar/gkad751. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Inhibitor
General Function
Catalyzes the oxidative deamination of primary and some secondary amine such as neurotransmitters, with concomitant reduction of oxygen to hydrogen peroxide and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues (PubMed:18391214, PubMed:20493079, PubMed:24169519, PubMed:8316221). Preferentially oxidizes serotonin (PubMed:20493079, PubMed:24169519). Also catalyzes the oxidative deamination of kynuramine to 3-(2-aminophenyl)-3-oxopropanal that can spontaneously condense to 4-hydroxyquinoline (By similarity)
Specific Function
Aliphatic amine oxidase activity
Gene Name
MAOA
Uniprot ID
P21397
Uniprot Name
Amine oxidase [flavin-containing] A
Molecular Weight
59681.27 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
  4. Zhou Y, Zhang Y, Zhao D, Yu X, Shen X, Zhou Y, Wang S, Qiu Y, Chen Y, Zhu F: TTD: Therapeutic Target Database describing target druggability information. Nucleic Acids Res. 2024 Jan 5;52(D1):D1465-D1477. doi: 10.1093/nar/gkad751. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Inhibitor
General Function
Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form (PubMed:8577704). Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis (Probable). Also has reductase activity on hydrogen peroxide (H2O2) (PubMed:10849437)
Specific Function
Fad binding
Gene Name
TXNRD1
Uniprot ID
Q16881
Uniprot Name
Thioredoxin reductase 1, cytoplasmic
Molecular Weight
70905.58 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
  4. Zhou Y, Zhang Y, Zhao D, Yu X, Shen X, Zhou Y, Wang S, Qiu Y, Chen Y, Zhu F: TTD: Therapeutic Target Database describing target druggability information. Nucleic Acids Res. 2024 Jan 5;52(D1):D1465-D1477. doi: 10.1093/nar/gkad751. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Inhibitor
General Function
Catalyzes the oxidative deamination of primary and some secondary amines such as neurotransmitters, and exogenous amines including the tertiary amine, neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), with concomitant reduction of oxygen to hydrogen peroxide and participates in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues (PubMed:11049757, PubMed:11134050, PubMed:20493079, PubMed:8316221, PubMed:8665924). Preferentially degrades benzylamine and phenylethylamine (PubMed:11049757, PubMed:11134050, PubMed:20493079, PubMed:8316221, PubMed:8665924)
Specific Function
Aliphatic amine oxidase activity
Gene Name
MAOB
Uniprot ID
P27338
Uniprot Name
Amine oxidase [flavin-containing] B
Molecular Weight
58762.475 Da
References
  1. Zhou Y, Zhang Y, Zhao D, Yu X, Shen X, Zhou Y, Wang S, Qiu Y, Chen Y, Zhu F: TTD: Therapeutic Target Database describing target druggability information. Nucleic Acids Res. 2024 Jan 5;52(D1):D1465-D1477. doi: 10.1093/nar/gkad751. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Cofactor
General Function
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Required for proper complex I assembly (PubMed:28671271). Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
Specific Function
Nadh dehydrogenase (ubiquinone) activity
Gene Name
NDUFA9
Uniprot ID
Q16795
Uniprot Name
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
Molecular Weight
42509.18 Da
References
  1. Bhatia C, Oerum S, Bray J, Kavanagh KL, Shafqat N, Yue W, Oppermann U: Towards a systematic analysis of human short-chain dehydrogenases/reductases (SDR): Ligand identification and structure-activity relationships. Chem Biol Interact. 2015 Jun 5;234:114-25. doi: 10.1016/j.cbi.2014.12.013. Epub 2014 Dec 16. [Article]
Kind
Protein
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pharmacological action
Unknown
General Function
Monooxygenase activity
Specific Function
Not Available
Gene Name
pobA
Uniprot ID
P20586
Uniprot Name
p-hydroxybenzoate hydroxylase
Molecular Weight
44323.175 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Pseudomonas fluorescens
Pharmacological action
Unknown
General Function
Fad binding
Specific Function
Not Available
Gene Name
pobA
Uniprot ID
P00438
Uniprot Name
p-hydroxybenzoate hydroxylase
Molecular Weight
44321.205 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Shewanella oneidensis (strain MR-1)
Pharmacological action
Unknown
General Function
Succinate dehydrogenase activity
Specific Function
Catalyzes fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown, but evidence indicates that flavocytochrome c participates in electron...
Gene Name
Not Available
Uniprot ID
P83223
Uniprot Name
Fumarate reductase flavoprotein subunit
Molecular Weight
62447.475 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Other protein disulfide isomerase family members can also be reoxidized, but at lower rates compared to P4HB, including PDIA2 (50% of P4HB reoxidation rate), as well as PDIA3, PDIA4, PDIA6 and NXNDC12 (<10%). Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. May be involved in oxidative proinsulin folding in pancreatic cells, hence may play a role in glucose homeostasis
Specific Function
Fad binding
Gene Name
ERO1B
Uniprot ID
Q86YB8
Uniprot Name
ERO1-like protein beta
Molecular Weight
53542.62 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
Kind
Protein
Organism
Mycobacterium tuberculosis
Pharmacological action
Unknown
General Function
May serve as electron transfer protein and supply electrons to P450 systems.
Specific Function
Ferredoxin-nad+ reductase activity
Gene Name
fprA
Uniprot ID
P9WIQ3
Uniprot Name
NADPH-ferredoxin reductase FprA
Molecular Weight
49340.605 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Catalyzes the reduction of two molecules of cytochrome b5 using NADH as the electron donor
Specific Function
Adp binding
Gene Name
CYB5R3
Uniprot ID
P00387
Uniprot Name
NADH-cytochrome b5 reductase 3
Molecular Weight
34234.55 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
Kind
Protein
Organism
Streptomyces sp. (strain SA-COO)
Pharmacological action
Unknown
General Function
Steroid delta-isomerase activity
Specific Function
Bifunctional enzyme that catalyzes the oxidation of the 3-beta-hydroxy group of cholesterol and the isomerization of the double bond of the resulting product.
Gene Name
choA
Uniprot ID
P12676
Uniprot Name
Cholesterol oxidase
Molecular Weight
58993.275 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Pharmacological action
Unknown
General Function
Thymidylate synthase (fad) activity
Specific Function
Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate.
Gene Name
thyX
Uniprot ID
Q9WYT0
Uniprot Name
Thymidylate synthase ThyX
Molecular Weight
26003.785 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Pharmacological action
Unknown
General Function
Thiamine pyrophosphate binding
Specific Function
Important for the aerobic growth. Decarboxylates pyruvate in four steps. The energy released is partially stored in acetyl phosphate.
Gene Name
pox5
Uniprot ID
P37063
Uniprot Name
Pyruvate oxidase
Molecular Weight
66110.5 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Unknown
General Function
Nadp binding
Specific Function
Maintains high levels of reduced glutathione in the cytosol.
Gene Name
gor
Uniprot ID
P06715
Uniprot Name
Glutathione reductase
Molecular Weight
48772.195 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Bacillus sp. (strain B-0618)
Pharmacological action
Unknown
General Function
Sarcosine oxidase activity
Specific Function
Catalyzes the oxidative demethylation of sarcosine. Can also oxidize other secondary amino acids such as N-methyl-L-alanine.
Gene Name
soxA
Uniprot ID
P40859
Uniprot Name
Monomeric sarcosine oxidase
Molecular Weight
43181.395 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Trypanosoma cruzi
Pharmacological action
Unknown
General Function
Trypanothione-disulfide reductase activity
Specific Function
Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.
Gene Name
TPR
Uniprot ID
P28593
Uniprot Name
Trypanothione reductase
Molecular Weight
53867.475 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Catalyzes the conversion of isovaleryl-CoA/3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA as an intermediate step in the leucine (Leu) catabolic pathway (PubMed:7640268). To a lesser extent, is also able to catalyze the oxidation of other saturated short-chain acyl-CoA thioesters as pentanoyl-CoA, hexenoyl-CoA and butenoyl-CoA (PubMed:7640268)
Specific Function
Butyryl-coa dehydrogenase activity
Gene Name
IVD
Uniprot ID
P26440
Uniprot Name
Isovaleryl-CoA dehydrogenase, mitochondrial
Molecular Weight
46650.435 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Brevibacterium sterolicum
Pharmacological action
Unknown
General Function
Steroid delta-isomerase activity
Specific Function
Catalyzes the oxidation and isomerization of cholesterol to cholestenone (4-cholesten-3-one), which is an initial step in the cholesterol degradation process.
Gene Name
choB
Uniprot ID
P22637
Uniprot Name
Cholesterol oxidase
Molecular Weight
59357.765 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Unknown
General Function
Oxidoreductase activity, acting on the ch-oh group of donors, quinone or similar compound as acceptor
Specific Function
First component of the membrane-bound D-lactate oxidase, which is believed to play an important role in the energization of the active transport of a variety of sugars and amino acids.
Gene Name
dld
Uniprot ID
P06149
Uniprot Name
D-lactate dehydrogenase
Molecular Weight
64611.82 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Isobutyryl-CoA dehydrogenase which catalyzes the conversion of 2-methylpropanoyl-CoA to (2E)-2-methylpropenoyl-CoA in the valine catabolic pathway (PubMed:11013134, PubMed:12359132, PubMed:16857760). To a lesser extent, also able to catalyze the oxidation of (2S)-2-methylbutanoyl-CoA (PubMed:11013134, PubMed:12359132)
Specific Function
2-methylpropanoyl-coa dehydrogenase activity
Gene Name
ACAD8
Uniprot ID
Q9UKU7
Uniprot Name
Isobutyryl-CoA dehydrogenase, mitochondrial
Molecular Weight
45069.39 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Functions both as NADH oxidoreductase and as regulator of apoptosis (PubMed:17094969, PubMed:20362274, PubMed:23217327, PubMed:33168626). In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase-independent pathway (PubMed:20362274). Release into the cytoplasm is mediated upon binding to poly-ADP-ribose chains (By similarity). The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA (PubMed:20362274). Binds to DNA in a sequence-independent manner (PubMed:27178839). Interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates caspase-7 to amplify apoptosis (PubMed:17094969). Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells (PubMed:19418225). In contrast, participates in normal mitochondrial metabolism. Plays an important role in the regulation of respiratory chain biogenesis by interacting with CHCHD4 and controlling CHCHD4 mitochondrial import (PubMed:26004228)
Specific Function
Dna binding
Gene Name
AIFM1
Uniprot ID
O95831
Uniprot Name
Apoptosis-inducing factor 1, mitochondrial
Molecular Weight
66900.09 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Unknown
General Function
Udp-galactopyranose mutase activity
Specific Function
Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF).
Gene Name
glf
Uniprot ID
P37747
Uniprot Name
UDP-galactopyranose mutase
Molecular Weight
42965.62 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Pharmacological action
Unknown
General Function
Oxygen transporter activity
Specific Function
Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from var...
Gene Name
hmp
Uniprot ID
P39662
Uniprot Name
Flavohemoprotein
Molecular Weight
44781.75 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Bacillus subtilis (strain 168)
Pharmacological action
Unknown
General Function
Glycine oxidase activity
Specific Function
Catalyzes the FAD-dependent oxidative deamination of various amines and D-amino acids to yield the corresponding alpha-keto acids, ammonia/amine, and hydrogen peroxide. Oxidizes sarcosine (N-methyl...
Gene Name
thiO
Uniprot ID
O31616
Uniprot Name
Glycine oxidase
Molecular Weight
40936.53 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5
Specific Function
Flavin adenine dinucleotide binding
Gene Name
POR
Uniprot ID
P16435
Uniprot Name
NADPH--cytochrome P450 reductase
Molecular Weight
76689.12 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive
Specific Function
Fatty-acyl-coa binding
Gene Name
GCDH
Uniprot ID
Q92947
Uniprot Name
Glutaryl-CoA dehydrogenase, mitochondrial
Molecular Weight
48126.715 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Medium-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (PubMed:1970566, PubMed:21237683, PubMed:2251268, PubMed:8823175). The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (PubMed:2251268). Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (PubMed:15159392, PubMed:25416781). Among the different mitochondrial acyl-CoA dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 6 to 12 carbons long primary chains (PubMed:1970566, PubMed:21237683, PubMed:2251268, PubMed:8823175)
Specific Function
Acyl-coa dehydrogenase activity
Gene Name
ACADM
Uniprot ID
P11310
Uniprot Name
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Molecular Weight
46587.98 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity (PubMed:16616139, PubMed:17088322, PubMed:17303072, PubMed:18544534, PubMed:20368421, PubMed:20567862, PubMed:20603179, PubMed:22203986, PubMed:23219954, PubMed:23391306, PubMed:25030849, PubMed:25701391, PubMed:29274788, PubMed:29326945, PubMed:30938755, PubMed:31799256, PubMed:32730563, PubMed:33484270, PubMed:34041270, PubMed:37558109, PubMed:38035964). Required to catabolize D-amino acids synthesized endogenously, of gastrointestinal bacterial origin or obtained from the diet, and to use these as nutrients (By similarity). Regulates the level of D-amino acid neurotransmitters in the brain, such as D-serine, a co-agonist of N-methyl D-aspartate (NMDA) receptors, and may modulate synaptic transmission (PubMed:17303072). Catalyzes the first step of the racemization of D-DOPA to L-DOPA, for possible use in an alternative dopamine biosynthesis pathway (PubMed:17303072). Also catalyzes the first step of the chiral inversion of N(gamma)-nitro-D-arginine methyl ester (D-NNA) to its L-enantiomer L-NNA that acts as a nitric oxide synthase inhibitor (By similarity). The hydrogen peroxide produced in the reaction provides protection against microbial infection; it contributes to the oxidative killing activity of phagocytic leukocytes and protects against bacterial colonization of the small intestine (By similarity). Enzyme secreted into the lumen of the intestine may not be catalytically active and could instead be proteolytically cleaved into peptides with antimicrobial activity (By similarity). The hydrogen peroxide produced in the reaction may also play a role in promoting cellular senescence in response to DNA damage (PubMed:30659069). Could act as a detoxifying agent which removes D-amino acids accumulated during aging (PubMed:17303072)
Specific Function
D-amino-acid oxidase activity
Gene Name
DAO
Uniprot ID
P14920
Uniprot Name
D-amino-acid oxidase
Molecular Weight
39473.75 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Unknown
General Function
Transcriptional repressor activity, bacterial-type rna polymerase core promoter proximal region sequence-specific binding
Specific Function
Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon.
Gene Name
putA
Uniprot ID
P09546
Uniprot Name
Bifunctional protein PutA
Molecular Weight
143813.665 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Pharmacological action
Unknown
General Function
Nucleotide binding
Specific Function
Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between...
Gene Name
phr
Uniprot ID
P61497
Uniprot Name
Deoxyribodipyrimidine photo-lyase
Molecular Weight
47900.455 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (By similarity). The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (By similarity). Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains (PubMed:11134486, PubMed:21237683)
Specific Function
Acyl-coa dehydrogenase activity
Gene Name
ACADS
Uniprot ID
P16219
Uniprot Name
Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Molecular Weight
44296.705 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Secreted L-amino-acid oxidase that acts as a key immunoregulator (PubMed:17356132, PubMed:32818467, PubMed:32866000). Has preference for L-aromatic amino acids: converts phenylalanine (Phe), tyrosine (Tyr) and tryptophan (Trp) to phenylpyruvic acid (PP), hydroxyphenylpyruvic acid (HPP), and indole-3-pyruvic acid (I3P), respectively (PubMed:17356132, PubMed:32818467, PubMed:32866000). Also has weak L-arginine oxidase activity (PubMed:26673964). Acts as a negative regulator of anti-tumor immunity by mediating Trp degradation via an indole pyruvate pathway that activates the transcription factor AHR (PubMed:32818467, PubMed:32866000). IL4I1-mediated Trp catabolism generates I3P, giving rise to indole metabolites (indole-3-acetic acid (IAA) and indole-3-aldehyde (I3A)) and kynurenic acid, which act as ligands for AHR, a ligand-activated transcription factor that plays important roles in immunity and cancer (PubMed:32818467, PubMed:32866000). AHR activation by indoles following IL4I1-mediated Trp degradation enhances tumor progression by promoting cancer cell motility and suppressing adaptive immunity (PubMed:32818467). Also has an immunoregulatory function in some immune cells, probably by mediating Trp degradation and promoting downstream AHR activation: inhibits T-cell activation and proliferation, promotes the differentiation of naive CD4(+) T-cells into FOXP3(+) regulatory T-cells (Treg) and regulates the development and function of B-cells (PubMed:17356132, PubMed:25446972, PubMed:25778793, PubMed:28891065). Also regulates M2 macrophage polarization by inhibiting T-cell activation (By similarity). Also has antibacterial properties by inhibiting growth of Gram negative and Gram positive bacteria through the production of NH4(+) and H2O2 (PubMed:23355881)
Specific Function
L-amino-acid oxidase activity
Gene Name
IL4I1
Uniprot ID
Q96RQ9
Uniprot Name
L-amino-acid oxidase
Molecular Weight
62880.52 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
  3. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Unknown
General Function
Nadph dehydrogenase activity
Specific Function
Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-2- enoyl-CoA.
Gene Name
fadH
Uniprot ID
P42593
Uniprot Name
2,4-dienoyl-CoA reductase [NADPH]
Molecular Weight
72677.545 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Pharmacological action
Unknown
General Function
Flavin adenine dinucleotide binding
Specific Function
Catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and fre...
Gene Name
xecC
Uniprot ID
Q56839
Uniprot Name
2-oxopropyl-CoM reductase, carboxylating
Molecular Weight
57347.19 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Shewanella frigidimarina
Pharmacological action
Unknown
General Function
Succinate dehydrogenase activity
Specific Function
Catalyzes fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown, but evidence indicates that flavocytochrome c participates in electron...
Gene Name
fccA
Uniprot ID
P0C278
Uniprot Name
Fumarate reductase flavoprotein subunit
Molecular Weight
60620.95 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Unknown
General Function
Thioredoxin-disulfide reductase activity
Specific Function
Not Available
Gene Name
trxB
Uniprot ID
P0A9P4
Uniprot Name
Thioredoxin reductase
Molecular Weight
34622.76 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Unknown
General Function
Methylenetetrahydrofolate reductase (nad(p)h) activity
Specific Function
Methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine.
Gene Name
metF
Uniprot ID
P0AEZ1
Uniprot Name
5,10-methylenetetrahydrofolate reductase
Molecular Weight
33102.375 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
Kind
Protein
Organism
Arthrobacter globiformis
Pharmacological action
Unknown
General Function
Nucleotide binding
Specific Function
Catalyzes the oxidative demethylation of N,N-dimethylglycine to yield sarcosine, formaldehyde and hydrogen peroxide. The oxidation of dimethylglycine is coupled to the synthesis of 5,10-methylenete...
Gene Name
dmg
Uniprot ID
Q9AGP8
Uniprot Name
Dimethylglycine oxidase
Molecular Weight
89983.935 Da
Kind
Protein
Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Pharmacological action
Unknown
General Function
Nadh peroxidase activity
Specific Function
Peroxidase whose active site is a redox-active cysteine-sulfenic acid.
Gene Name
npr
Uniprot ID
P37062
Uniprot Name
NADH peroxidase
Molecular Weight
49565.17 Da
Kind
Protein
Organism
Anabaena sp. (strain PCC 7119)
Pharmacological action
Unknown
General Function
Nadp binding
Specific Function
Not Available
Gene Name
petH
Uniprot ID
P21890
Uniprot Name
Ferredoxin--NADP reductase
Molecular Weight
48865.145 Da
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Unknown
General Function
Sulfite reductase (nadph) activity
Specific Function
Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate....
Gene Name
cysJ
Uniprot ID
P38038
Uniprot Name
Sulfite reductase [NADPH] flavoprotein alpha-component
Molecular Weight
66269.23 Da
Kind
Protein
Organism
Azotobacter vinelandii
Pharmacological action
Unknown
General Function
Ferredoxin-nadp+ reductase activity
Specific Function
Not Available
Gene Name
fpr
Uniprot ID
Q44532
Uniprot Name
Ferredoxin--NADP reductase
Molecular Weight
29416.405 Da
Kind
Protein
Organism
Megasphaera elsdenii
Pharmacological action
Unknown
General Function
Flavin adenine dinucleotide binding
Specific Function
Has an optimum specificity for 4-carbon length fatty acyl-CoAs.
Gene Name
Not Available
Uniprot ID
Q06319
Uniprot Name
Acyl-CoA dehydrogenase, short-chain specific
Molecular Weight
41407.87 Da
Kind
Protein
Organism
Pseudomonas sp. (strain KKS102)
Pharmacological action
Unknown
General Function
Oxidoreductase activity
Specific Function
Not Available
Gene Name
bphA4
Uniprot ID
Q52437
Uniprot Name
Ferredoxin reductase
Molecular Weight
43172.815 Da
Kind
Protein
Organism
Azotobacter vinelandii
Pharmacological action
Unknown
General Function
Flavin adenine dinucleotide binding
Specific Function
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihy...
Gene Name
Not Available
Uniprot ID
P18925
Uniprot Name
Dihydrolipoyl dehydrogenase
Molecular Weight
49566.78 Da
Kind
Protein
Organism
Pseudomonas syringae pv. tomato (strain DC3000)
Pharmacological action
Unknown
General Function
Oxidoreductase activity
Specific Function
Not Available
Gene Name
Not Available
Uniprot ID
Q888A4
Uniprot Name
Amine oxidase, flavin-containing protein
Molecular Weight
35839.285 Da
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Unknown
General Function
Nucleotide binding
Specific Function
Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between...
Gene Name
phrB
Uniprot ID
P00914
Uniprot Name
Deoxyribodipyrimidine photo-lyase
Molecular Weight
53666.505 Da
Kind
Protein
Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Pharmacological action
Unknown
General Function
Nucleotide binding
Specific Function
Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between...
Gene Name
phr
Uniprot ID
P05327
Uniprot Name
Deoxyribodipyrimidine photo-lyase
Molecular Weight
54461.235 Da
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Unknown
General Function
L-aspartate:fumarate oxidoreductase activity
Specific Function
Catalyzes the oxidation of L-aspartate to iminoaspartate.
Gene Name
nadB
Uniprot ID
P10902
Uniprot Name
L-aspartate oxidase
Molecular Weight
60336.885 Da
Kind
Protein
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Pharmacological action
Unknown
General Function
Dna photolyase activity
Specific Function
May have a photoreceptor function. Binds DNA; represses transcription of at least 8 genes, including slr0364 and slr1866. Does not encode a DNA photolyase function. Its disruption does not affect c...
Gene Name
cry
Uniprot ID
P77967
Uniprot Name
Cryptochrome DASH
Molecular Weight
57039.58 Da
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (PubMed:15712224, PubMed:16442803, PubMed:16770810, PubMed:17404228, PubMed:20160912, PubMed:20385101). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (PubMed:29211711). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (PubMed:29211711). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity)
Specific Function
Dihydrolipoyl dehydrogenase activity
Gene Name
DLD
Uniprot ID
P09622
Uniprot Name
Dihydrolipoyl dehydrogenase, mitochondrial
Molecular Weight
54176.91 Da
References
  1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
Kind
Protein
Organism
Shewanella frigidimarina (strain NCIMB 400)
Pharmacological action
Unknown
General Function
Succinate dehydrogenase activity
Specific Function
Catalyzes unidirectional fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown.
Gene Name
ifcA
Uniprot ID
Q9Z4P0
Uniprot Name
Fumarate reductase flavoprotein subunit
Molecular Weight
62946.005 Da
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction
Specific Function
Cytochrome-b5 reductase activity, acting on nad(p)h
Gene Name
CYB5R1
Uniprot ID
Q9UHQ9
Uniprot Name
NADH-cytochrome b5 reductase 1
Molecular Weight
34094.57 Da
References
  1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
Kind
Protein
Organism
Brevibacterium sterolicum
Pharmacological action
Unknown
General Function
Oxidoreductase activity, acting on ch-oh group of donors
Specific Function
Not Available
Gene Name
Not Available
Uniprot ID
Q7SID9
Uniprot Name
Oxidoreductase
Molecular Weight
61519.03 Da
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Serves as the first electron transfer protein in all the mitochondrial P450 systems including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver
Specific Function
Ferredoxin-nadp+ reductase activity
Gene Name
FDXR
Uniprot ID
P22570
Uniprot Name
NADPH:adrenodoxin oxidoreductase, mitochondrial
Molecular Weight
53836.36 Da
References
  1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Involved in the initial and rate-limiting step of peroxisomal beta-oxidation of straight-chain saturated and unsaturated very-long-chain fatty acids (PubMed:15060085, PubMed:17458872, PubMed:17603022, PubMed:32169171, PubMed:33234382, PubMed:7876265). Catalyzes the desaturation of fatty acyl-CoAs such as palmitoyl-CoA (hexadecanoyl-CoA) to 2-trans-enoyl-CoAs ((2E)-enoyl-CoAs) such as (2E)-hexadecenoyl-CoA, and donates electrons directly to molecular oxygen (O(2)), thereby producing hydrogen peroxide (H(2)O(2)) (PubMed:17458872, PubMed:17603022, PubMed:7876265)
Specific Function
Acyl-coa oxidase activity
Gene Name
ACOX1
Uniprot ID
Q15067
Uniprot Name
Peroxisomal acyl-coenzyme A oxidase 1
Molecular Weight
74423.035 Da
References
  1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Unknown
General Function
Udp-n-acetylmuramate dehydrogenase activity
Specific Function
Cell wall formation.
Gene Name
murB
Uniprot ID
P08373
Uniprot Name
UDP-N-acetylenolpyruvoylglucosamine reductase
Molecular Weight
37850.835 Da
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen
Specific Function
Flavin adenine dinucleotide binding
Gene Name
GFER
Uniprot ID
P55789
Uniprot Name
FAD-linked sulfhydryl oxidase ALR
Molecular Weight
23448.95 Da
References
  1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
Kind
Protein
Organism
Staphylococcus aureus (strain MW2)
Pharmacological action
Unknown
General Function
Udp-n-acetylmuramate dehydrogenase activity
Specific Function
Cell wall formation.
Gene Name
murB
Uniprot ID
P61432
Uniprot Name
UDP-N-acetylenolpyruvoylglucosamine reductase
Molecular Weight
33797.18 Da
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Unknown
General Function
Oxygen transporter activity
Specific Function
Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from var...
Gene Name
hmp
Uniprot ID
P24232
Uniprot Name
Flavohemoprotein
Molecular Weight
43867.385 Da
Kind
Protein
Organism
Bacillus thermoglucosidasius
Pharmacological action
Unknown
General Function
Oxidoreductase activity
Specific Function
Not Available
Gene Name
pheA2
Uniprot ID
Q9LAG2
Uniprot Name
Phenol 2-hydroxylase component B
Molecular Weight
17658.25 Da
Kind
Protein
Organism
Thermus thermophilus
Pharmacological action
Unknown
General Function
Nucleotide binding
Specific Function
Not Available
Gene Name
metF
Uniprot ID
Q9RA47
Uniprot Name
Methylenetetrahydrofolate reductase
Molecular Weight
25475.8 Da
Kind
Protein
Organism
Pseudomonas putida
Pharmacological action
Unknown
General Function
Oxidoreductase activity
Specific Function
The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electron...
Gene Name
camA
Uniprot ID
P16640
Uniprot Name
Putidaredoxin reductase
Molecular Weight
45578.655 Da
Kind
Protein
Organism
Mycobacterium tuberculosis
Pharmacological action
Unknown
General Function
May contribute to virulence by increasing resistance to reactive oxygen intermediates. It can reduce 2,6-dimethyl-1,4-benzoquinone (DMBQ), 5-hydroxy-1,4-naphthaquinone (5-HNQ) and menadione. NADPH is the physiological reductant rather than NADH.
Specific Function
Flavin adenine dinucleotide binding
Gene Name
lpdA
Uniprot ID
P9WHH7
Uniprot Name
NAD(P)H dehydrogenase (quinone)
Molecular Weight
51488.44 Da
Kind
Protein
Organism
Mycobacterium tuberculosis
Pharmacological action
Unknown
General Function
Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF) which is a key building block for cell wall construction in Mycobacterium tuberculosis.
Specific Function
Udp-galactopyranose mutase activity
Gene Name
glf
Uniprot ID
P9WIQ1
Uniprot Name
UDP-galactopyranose mutase
Molecular Weight
45814.07 Da
Kind
Protein
Organism
Clostridium aminobutyricum
Pharmacological action
Unknown
General Function
Vinylacetyl-coa delta-isomerase activity
Specific Function
Catalyzes the reversible conversion of 4-hydroxybutyryl-CoA to crotonyl-CoA. The mechanism of the reaction seems to go through three steps: (1) the FAD-dependent oxidation of 4-hydroxybutyryl-CoA t...
Gene Name
abfD
Uniprot ID
P55792
Uniprot Name
4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA-Delta-isomerase
Molecular Weight
54421.685 Da
Kind
Protein
Organism
Pseudomonas putida
Pharmacological action
Unknown
General Function
Oxidoreductase activity, acting on ch-oh group of donors
Specific Function
Not Available
Gene Name
pchF
Uniprot ID
P09788
Uniprot Name
4-cresol dehydrogenase [hydroxylating] flavoprotein subunit
Molecular Weight
57944.95 Da
Kind
Protein
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Pharmacological action
Unknown
General Function
Protein disulfide oxidoreductase activity
Specific Function
Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined ...
Gene Name
ahpF
Uniprot ID
P19480
Uniprot Name
Alkyl hydroperoxide reductase subunit F
Molecular Weight
55949.41 Da
Kind
Protein
Organism
Neisseria meningitidis
Pharmacological action
Unknown
General Function
Flavin adenine dinucleotide binding
Specific Function
Not Available
Gene Name
m-6
Uniprot ID
Q51225
Uniprot Name
Dihydrolipoyl dehydrogenase
Molecular Weight
61882.415 Da
Kind
Protein
Organism
Plasmodium falciparum (isolate K1 / Thailand)
Pharmacological action
Unknown
General Function
Glutathione-disulfide reductase activity
Specific Function
Maintains high levels of reduced glutathione in the cytosol.
Gene Name
GR2
Uniprot ID
Q94655
Uniprot Name
Glutathione reductase
Molecular Weight
56560.695 Da
Kind
Protein
Organism
Thermobifida fusca (strain YX)
Pharmacological action
Unknown
General Function
Phenylacetone monooxygenase activity
Specific Function
Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Is most efficient with pheny...
Gene Name
pamO
Uniprot ID
Q47PU3
Uniprot Name
Phenylacetone monooxygenase
Molecular Weight
61123.225 Da
Kind
Protein
Organism
Acinetobacter sp. (strain ADP1)
Pharmacological action
Unknown
General Function
Metal ion binding
Specific Function
Electron transfer component of benzoate 1,2-dioxygenase system.
Gene Name
benC
Uniprot ID
P07771
Uniprot Name
Benzoate 1,2-dioxygenase electron transfer component
Molecular Weight
38782.465 Da
Kind
Protein
Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Pharmacological action
Unknown
General Function
Flavin adenine dinucleotide binding
Specific Function
Not Available
Gene Name
Not Available
Uniprot ID
Q72JJ3
Uniprot Name
Putative acyl-CoA dehydrogenase
Molecular Weight
42159.22 Da
Kind
Protein
Organism
Streptomyces hygroscopicus subsp. ascomyceticus
Pharmacological action
Unknown
General Function
Flavin adenine dinucleotide binding
Specific Function
Not Available
Gene Name
fkbI
Uniprot ID
Q9KIE5
Uniprot Name
FkbI
Molecular Weight
38183.945 Da
Kind
Protein
Organism
Pseudomonas putida
Pharmacological action
Unknown
General Function
Flavin adenine dinucleotide binding
Specific Function
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain...
Gene Name
lpdV
Uniprot ID
P09063
Uniprot Name
Dihydrolipoyl dehydrogenase
Molecular Weight
48158.33 Da
Kind
Protein
Organism
Pseudomonas fluorescens
Pharmacological action
Unknown
General Function
Flavin adenine dinucleotide binding
Specific Function
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain...
Gene Name
lpd
Uniprot ID
P14218
Uniprot Name
Dihydrolipoyl dehydrogenase
Molecular Weight
50150.535 Da
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Unknown
General Function
Protein disulfide oxidoreductase activity
Specific Function
Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined ...
Gene Name
ahpF
Uniprot ID
P35340
Uniprot Name
Alkyl hydroperoxide reductase subunit F
Molecular Weight
56176.63 Da
Kind
Protein
Organism
Nostoc sp. (strain PCC 7120 / UTEX 2576)
Pharmacological action
Unknown
General Function
Ferredoxin-nadp+ reductase activity
Specific Function
Not Available
Gene Name
petH
Uniprot ID
P58558
Uniprot Name
Ferredoxin--NADP reductase
Molecular Weight
48838.075 Da
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Unknown
General Function
Oxidoreductase activity
Specific Function
Transports electrons between flavodoxin or ferredoxin and NADPH. Involved in the reductive activation of cobalamin-independent methionine synthase, pyruvate formate lyase and anaerobic ribonucleoti...
Gene Name
fpr
Uniprot ID
P28861
Uniprot Name
Ferredoxin--NADP reductase
Molecular Weight
27750.735 Da
Kind
Protein
Organism
Bacillus sp. (strain HIL-Y85/54728)
Pharmacological action
Unknown
General Function
Oxidoreductase activity
Specific Function
Catalyzes the oxidative decarboxylation of the C-terminal cysteine residue of mersacidin to an aminoenethiol residue.
Gene Name
mrsD
Uniprot ID
Q9RC23
Uniprot Name
Mersacidin decarboxylase
Molecular Weight
21677.045 Da

Enzymes

Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Catalyzes the oxidative deamination of primary and some secondary amines such as neurotransmitters, and exogenous amines including the tertiary amine, neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), with concomitant reduction of oxygen to hydrogen peroxide and participates in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues (PubMed:11049757, PubMed:11134050, PubMed:20493079, PubMed:8316221, PubMed:8665924). Preferentially degrades benzylamine and phenylethylamine (PubMed:11049757, PubMed:11134050, PubMed:20493079, PubMed:8316221, PubMed:8665924)
Specific Function
Aliphatic amine oxidase activity
Gene Name
MAOB
Uniprot ID
P27338
Uniprot Name
Amine oxidase [flavin-containing] B
Molecular Weight
58762.475 Da
References
  1. Edmondson DE, Binda C, Mattevi A: The FAD binding sites of human monoamine oxidases A and B. Neurotoxicology. 2004 Jan;25(1-2):63-72. doi: 10.1016/S0161-813X(03)00114-1. [Article]
  2. Edmondson DE, Newton-Vinson P: The covalent FAD of monoamine oxidase: structural and functional role and mechanism of the flavinylation reaction. Antioxid Redox Signal. 2001 Oct;3(5):789-806. doi: 10.1089/15230860152664984. [Article]
  3. Guerin JF, Ouhibi N, Regnier-Vigouroux G, Menezo Y: Movement characteristics and hyperactivation of human sperm on different epithelial cell monolayers. Int J Androl. 1991 Dec;14(6):412-22. [Article]
  4. Gerlach M, Riederer P, Youdim MB: The molecular pharmacology of L-deprenyl. Eur J Pharmacol. 1992 Jun 5;226(2):97-108. doi: 10.1016/0922-4106(92)90170-z. [Article]

Drug created at June 13, 2005 13:24 / Updated at September 16, 2024 01:20