Flavin adenine dinucleotide
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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.
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- Contraindications & Blackbox Warnings
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- Pharmacodynamics
Not Available
- Mechanism of action
Target Actions Organism ARibosyldihydronicotinamide dehydrogenase [quinone] inhibitorHumans ANitric oxide synthase 1 inhibitorHumans ADihydropyrimidine dehydrogenase [NADP(+)] inhibitorHumans AXanthine dehydrogenase/oxidase inhibitorHumans AGlutathione reductase, mitochondrial inhibitorHumans ANAD(P)H dehydrogenase [quinone] 1 inhibitorHumans AAmine oxidase [flavin-containing] A inhibitorHumans AThioredoxin reductase 1, cytoplasmic inhibitorHumans AAmine oxidase [flavin-containing] B inhibitorHumans UNADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial cofactorHumans Up-hydroxybenzoate hydroxylase Not Available Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) Up-hydroxybenzoate hydroxylase Not Available Pseudomonas fluorescens UFumarate reductase flavoprotein subunit Not Available Shewanella oneidensis (strain MR-1) UERO1-like protein beta Not Available Humans UNADPH-ferredoxin reductase FprA Not Available Mycobacterium tuberculosis UNADH-cytochrome b5 reductase 3 Not Available Humans UCholesterol oxidase Not Available Streptomyces sp. (strain SA-COO) UThymidylate synthase ThyX Not Available Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) UPyruvate oxidase Not Available Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) UGlutathione reductase Not Available Escherichia coli (strain K12) UMonomeric sarcosine oxidase Not Available Bacillus sp. (strain B-0618) UTrypanothione reductase Not Available Trypanosoma cruzi UIsovaleryl-CoA dehydrogenase, mitochondrial Not Available Humans UCholesterol oxidase Not Available Brevibacterium sterolicum UD-lactate dehydrogenase Not Available Escherichia coli (strain K12) UIsobutyryl-CoA dehydrogenase, mitochondrial Not Available Humans UApoptosis-inducing factor 1, mitochondrial Not Available Humans UUDP-galactopyranose mutase Not Available Escherichia coli (strain K12) UFlavohemoprotein Not Available Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) UGlycine oxidase Not Available Bacillus subtilis (strain 168) UNADPH--cytochrome P450 reductase Not Available Humans UGlutaryl-CoA dehydrogenase, mitochondrial Not Available Humans UMedium-chain specific acyl-CoA dehydrogenase, mitochondrial Not Available Humans UD-amino-acid oxidase Not Available Humans UBifunctional protein PutA Not Available Escherichia coli (strain K12) UDeoxyribodipyrimidine photo-lyase Not Available Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) UShort-chain specific acyl-CoA dehydrogenase, mitochondrial Not Available Humans UL-amino-acid oxidase Not Available Humans U2,4-dienoyl-CoA reductase [NADPH] Not Available Escherichia coli (strain K12) U2-oxopropyl-CoM reductase, carboxylating Not Available Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) UFumarate reductase flavoprotein subunit Not Available Shewanella frigidimarina UThioredoxin reductase Not Available Escherichia coli (strain K12) U5,10-methylenetetrahydrofolate reductase Not Available Escherichia coli (strain K12) UDimethylglycine oxidase Not Available Arthrobacter globiformis UNADH peroxidase Not Available Enterococcus faecalis (strain ATCC 700802 / V583) UFerredoxin--NADP reductase Not Available Anabaena sp. (strain PCC 7119) USulfite reductase [NADPH] flavoprotein alpha-component Not Available Escherichia coli (strain K12) UFerredoxin--NADP reductase Not Available Azotobacter vinelandii UAcyl-CoA dehydrogenase, short-chain specific Not Available Megasphaera elsdenii UFerredoxin reductase Not Available Pseudomonas sp. (strain KKS102) UDihydrolipoyl dehydrogenase Not Available Azotobacter vinelandii UAmine oxidase, flavin-containing protein Not Available Pseudomonas syringae pv. tomato (strain DC3000) UDeoxyribodipyrimidine photo-lyase Not Available Escherichia coli (strain K12) UDeoxyribodipyrimidine photo-lyase Not Available Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) UL-aspartate oxidase Not Available Escherichia coli (strain K12) UCryptochrome DASH Not Available Synechocystis sp. (strain PCC 6803 / Kazusa) UDihydrolipoyl dehydrogenase, mitochondrial Not Available Humans UFumarate reductase flavoprotein subunit Not Available Shewanella frigidimarina (strain NCIMB 400) UNADH-cytochrome b5 reductase 1 Not Available Humans UOxidoreductase Not Available Brevibacterium sterolicum UNADPH:adrenodoxin oxidoreductase, mitochondrial Not Available Humans UPeroxisomal acyl-coenzyme A oxidase 1 Not Available Humans UUDP-N-acetylenolpyruvoylglucosamine reductase Not Available Escherichia coli (strain K12) UFAD-linked sulfhydryl oxidase ALR Not Available Humans UUDP-N-acetylenolpyruvoylglucosamine reductase Not Available Staphylococcus aureus (strain MW2) UFlavohemoprotein Not Available Escherichia coli (strain K12) UPhenol 2-hydroxylase component B Not Available Bacillus thermoglucosidasius UMethylenetetrahydrofolate reductase Not Available Thermus thermophilus UPutidaredoxin reductase Not Available Pseudomonas putida UNAD(P)H dehydrogenase (quinone) Not Available Mycobacterium tuberculosis UUDP-galactopyranose mutase Not Available Mycobacterium tuberculosis U4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA-Delta-isomerase Not Available Clostridium aminobutyricum U4-cresol dehydrogenase [hydroxylating] flavoprotein subunit Not Available Pseudomonas putida UAlkyl hydroperoxide reductase subunit F Not Available Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) UDihydrolipoyl dehydrogenase Not Available Neisseria meningitidis UGlutathione reductase Not Available Plasmodium falciparum (isolate K1 / Thailand) UPhenylacetone monooxygenase Not Available Thermobifida fusca (strain YX) UBenzoate 1,2-dioxygenase electron transfer component Not Available Acinetobacter sp. (strain ADP1) UPutative acyl-CoA dehydrogenase Not Available Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) UFkbI Not Available Streptomyces hygroscopicus subsp. ascomyceticus UDihydrolipoyl dehydrogenase Not Available Pseudomonas putida UDihydrolipoyl dehydrogenase Not Available Pseudomonas fluorescens UAlkyl hydroperoxide reductase subunit F Not Available Escherichia coli (strain K12) UFerredoxin--NADP reductase Not Available Nostoc sp. (strain PCC 7120 / UTEX 2576) UFerredoxin--NADP reductase Not Available Escherichia coli (strain K12) UMersacidin decarboxylase Not Available Bacillus 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 outcomesWith structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!Improve decision support & research outcomes with our structured adverse effects data.
- Toxicity
Oral mouse LD50 > 7000 mg/kg. Intravenous mouse LD50 589 mg/kg.
- Pathways
- 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 regionsOur datasets provide approved product information including:dosage, form, labeller, route of administration, and marketing period.Access drug product information from over 10 global regions.
- Product Ingredients
Ingredient UNII CAS InChI Key Flavin adenine dinucleotide disodium 67U7UHJ04C 84366-81-4 XLRHXNIVIZZOON-WFUPGROFSA-N - International/Other Brands
- Adeflavin / Flaziren
- Mixture Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image PramLyte Flavin 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) Kit Oral Allegis Pharmaceuticals, LLC 2015-09-11 2016-01-04 US - Unapproved/Other Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image BumP DHA Flavin 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) Capsule Oral Centurion Labs 2017-03-24 2017-04-17 US EnBrace HR Flavin 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 pellets Oral Jaymac Pharmaceuticals Llc 2011-08-12 Not applicable US PaxLyte Flavin 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) Capsule Oral Jaymac Pharmaceuticals Llc 2024-08-01 Not applicable US
Categories
- Drug Categories
- Adenine Nucleotides
- Biological Factors
- Coenzymes
- Enzymes and Coenzymes
- Flavins
- Heterocyclic Compounds, Fused-Ring
- Monoamine Oxidase A Inhibitors for interaction with Monoamine Oxidase A substrates
- Nucleic Acids, Nucleotides, and Nucleosides
- Nucleotides
- Pigments, Biological
- Pteridines
- Purine Nucleotides
- Purines
- Ribonucleotides
- Vitamin B Complex
- Vitamins
- 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
- External Links
- Human Metabolome Database
- HMDB0001248
- KEGG Drug
- D00005
- KEGG Compound
- C00016
- PubChem Compound
- 643975
- PubChem Substance
- 46508543
- ChemSpider
- 559059
- 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 2878 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 Phase Status Purpose Conditions Count Start Date Why Stopped 100+ additional columns Unlock 175K+ rows when you subscribe.View sample data4 Withdrawn Treatment Menstrual Related Mood Disorder / Premenstrual Dysphoric Disorder (PMDD) / Premenstrual Syndrome (PMS) / Premenstrual tension with edema 1 somestatus stop reason just information to hide
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
Form Route Strength Capsule Oral Capsule, liquid filled Oral Capsule, delayed release pellets Oral Kit Oral - Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Solid
- Experimental Properties
- Not Available
- Predicted Properties
Property Value Source Water Solubility 4.25 mg/mL ALOGPS logP -0.78 ALOGPS logP -4.8 Chemaxon logS -2.3 ALOGPS pKa (Strongest Acidic) 1.85 Chemaxon pKa (Strongest Basic) 4.89 Chemaxon Physiological Charge -3 Chemaxon Hydrogen Acceptor Count 19 Chemaxon Hydrogen Donor Count 9 Chemaxon Polar Surface Area 356.42 Å2 Chemaxon Rotatable Bond Count 13 Chemaxon Refractivity 177.43 m3·mol-1 Chemaxon Polarizability 70.53 Å3 Chemaxon Number of Rings 6 Chemaxon Bioavailability 0 Chemaxon Rule of Five No Chemaxon Ghose Filter No Chemaxon Veber's Rule No Chemaxon MDDR-like Rule Yes Chemaxon - Predicted ADMET Features
Property Value Probability Human Intestinal Absorption - 0.6156 Blood Brain Barrier + 0.5 Caco-2 permeable - 0.6995 P-glycoprotein substrate Substrate 0.6464 P-glycoprotein inhibitor I Non-inhibitor 0.7931 P-glycoprotein inhibitor II Non-inhibitor 0.9705 Renal organic cation transporter Non-inhibitor 0.9561 CYP450 2C9 substrate Non-substrate 0.8093 CYP450 2D6 substrate Non-substrate 0.8312 CYP450 3A4 substrate Substrate 0.5632 CYP450 1A2 substrate Non-inhibitor 0.8426 CYP450 2C9 inhibitor Non-inhibitor 0.8818 CYP450 2D6 inhibitor Non-inhibitor 0.8636 CYP450 2C19 inhibitor Non-inhibitor 0.872 CYP450 3A4 inhibitor Non-inhibitor 0.7323 CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.8967 Ames test Non AMES toxic 0.8242 Carcinogenicity Non-carcinogens 0.8105 Biodegradation Not ready biodegradable 0.9965 Rat acute toxicity 2.5009 LD50, mol/kg Not applicable hERG inhibition (predictor I) Weak inhibitor 0.9501 hERG inhibition (predictor II) Inhibitor 0.578
Spectra
- Mass Spec (NIST)
- Not Available
- Spectra
- Chromatographic Properties
Collision Cross Sections (CCS)
Adduct CCS Value (â„«2) Source type Source [M-H]- 277.5674337 predictedDarkChem Lite v0.1.0 [M-H]- 273.0312337 predictedDarkChem Lite v0.1.0 [M-H]- 293.8611337 predictedDarkChem Lite v0.1.0 [M-H]- 243.13689 predictedDeepCCS 1.0 (2019) [M+H]+ 277.4043337 predictedDarkChem Lite v0.1.0 [M+H]+ 273.2360337 predictedDarkChem Lite v0.1.0 [M+H]+ 244.86061 predictedDeepCCS 1.0 (2019) [M+Na]+ 275.9832337 predictedDarkChem Lite v0.1.0 [M+Na]+ 272.8946337 predictedDarkChem Lite v0.1.0 [M+Na]+ 251.18956 predictedDeepCCS 1.0 (2019)
Targets
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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]
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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]
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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]
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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]
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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]
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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]
- 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
- 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
- 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
- Catalyzes the incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). The reaction occurs in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduced nicotinamide adenine dinucleotide phosphate (NADPH) in response to binding p-hydroxybenzoate to the enzyme and oxidation of reduced FAD with oxygen to form a hydroperoxide, which then oxygenates p-hydroxybenzoate.
- Specific Function
- 4-hydroxybenzoate 3-monooxygenase [NADPH] activity
- Gene Name
- pobA
- Uniprot ID
- P20586
- Uniprot Name
- p-hydroxybenzoate hydroxylase
- Molecular Weight
- 44323.175 Da
References
- Kind
- Protein
- Organism
- Pseudomonas fluorescens
- Pharmacological action
- Unknown
- General Function
- Catalyzes the incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). The reaction occurs in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduced nicotinamide adenine dinucleotide phosphate (NADPH) in response to binding p-hydroxybenzoate to the enzyme and oxidation of reduced FAD with oxygen to form a hydroperoxide, which then oxygenates p-hydroxybenzoate.
- Specific Function
- 4-hydroxybenzoate 3-monooxygenase [NADPH] activity
- Gene Name
- pobA
- Uniprot ID
- P00438
- Uniprot Name
- p-hydroxybenzoate hydroxylase
- Molecular Weight
- 44321.205 Da
References
- Kind
- Protein
- Organism
- Shewanella oneidensis (strain MR-1)
- Pharmacological action
- Unknown
- General Function
- Flavocytochrome that catalyzes the reduction of fumarate to succinate (PubMed:12196158, PubMed:12899636, PubMed:22458729). Is essential for fumarate respiration during anaerobic growth, acting as the terminal reductase (By similarity). Receives electrons from the membrane-bound tetraheme c-type cytochrome CymA (PubMed:12196158, PubMed:12899636, PubMed:19837833, PubMed:22458729). Under ferric iron-reducing conditions, can be part of an electron transport chain to ferric iron, by accepting electrons from CymA and transfering them to the c-type cytochrome MtrA (PubMed:19837833). Also plays an important role in the reduction of selenite to elemental selenium (PubMed:24435070). May act as a transient electron storage protein (PubMed:19837833).
- Specific Function
- FMN binding
- Gene Name
- Not Available
- Uniprot ID
- P83223
- Uniprot Name
- Fumarate reductase flavoprotein subunit
- Molecular Weight
- 62447.475 Da
References
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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
- Transports electrons between ferredoxin and NADPH. May supply electrons to P450 systems (PubMed:12071965). The enzyme can use both NADPH and NADH as a reductant, but the catalytic efficiency is two orders of magnitude higher with NADPH (PubMed:12071965).
- Specific Function
- ferredoxin-NAD+ reductase activity
- Gene Name
- fprA
- Uniprot ID
- P9WIQ3
- Uniprot Name
- NADPH-ferredoxin reductase FprA
- Molecular Weight
- 49340.605 Da
References
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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
- 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, producing cholest-4-en-3-one. These reactions are part of a cholesterol degradation pathway that allows the bacterium to utilize cholesterol as its sole source of carbon and energy.
- Specific Function
- cholesterol oxidase activity
- Gene Name
- choA
- Uniprot ID
- P12676
- Uniprot Name
- Cholesterol oxidase
- Molecular Weight
- 58993.275 Da
References
- Kind
- Protein
- Organism
- Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
- Pharmacological action
- Unknown
- General Function
- Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP or deoxyuridylate) to 2'-deoxythymidine-5'-monophosphate (dTMP or deoxythymidylate) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methylene donor, and NAD(P)H and FADH(2) as the reductant. This reaction is a critical step in DNA biosynthesis (PubMed:12791256, PubMed:19370033). Can also use formaldehyde instead of mTHF as a direct methylene donor for dTMP synthesis. However, the tighter binding of ThyX to mTHF (KD of 4 uM) compared to formaldehyde (KD of 20 mM) confirms that methylene tetrahydrofolate acts as the biological carbon donor for ThyX, serving as a formaldehyde carrier/transporter and thus avoiding genotoxic effects (PubMed:34315871).
- Specific Function
- flavin adenine dinucleotide binding
- Gene Name
- thyX
- Uniprot ID
- Q9WYT0
- Uniprot Name
- Thymidylate synthase ThyX
- Molecular Weight
- 26003.785 Da
References
- Kind
- Protein
- Organism
- Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
- Pharmacological action
- Unknown
- General Function
- Important for the aerobic growth. Decarboxylates pyruvate in four steps. The energy released is partially stored in acetyl phosphate.
- Specific Function
- magnesium ion binding
- Gene Name
- pox5
- Uniprot ID
- P37063
- Uniprot Name
- Pyruvate oxidase
- Molecular Weight
- 66110.5 Da
References
- Kind
- Protein
- Organism
- Escherichia coli (strain K12)
- Pharmacological action
- Unknown
- General Function
- Maintains high levels of reduced glutathione in the cytosol.
- Specific Function
- FAD binding
- Gene Name
- gor
- Uniprot ID
- P06715
- Uniprot Name
- Glutathione reductase
- Molecular Weight
- 48772.195 Da
References
- Kind
- Protein
- Organism
- Bacillus sp. (strain B-0618)
- Pharmacological action
- Unknown
- General Function
- Catalyzes the oxidative demethylation of sarcosine. Can also oxidize other secondary amino acids such as N-methyl-L-alanine.
- Specific Function
- flavin adenine dinucleotide binding
- Gene Name
- soxA
- Uniprot ID
- P40859
- Uniprot Name
- Monomeric sarcosine oxidase
- Molecular Weight
- 43181.395 Da
References
- Kind
- Protein
- Organism
- Trypanosoma cruzi
- Pharmacological action
- Unknown
- General Function
- Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.
- Specific Function
- flavin adenine dinucleotide binding
- Gene Name
- TPR
- Uniprot ID
- P28593
- Uniprot Name
- Trypanothione reductase
- Molecular Weight
- 53867.475 Da
References
- 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
- Kind
- Protein
- Organism
- Brevibacterium sterolicum
- Pharmacological action
- Unknown
- General Function
- Catalyzes the oxidation and isomerization of cholesterol to cholestenone (4-cholesten-3-one), which is an initial step in the cholesterol degradation process.
- Specific Function
- cholesterol oxidase activity
- Gene Name
- choB
- Uniprot ID
- P22637
- Uniprot Name
- Cholesterol oxidase
- Molecular Weight
- 59357.765 Da
References
- Kind
- Protein
- Organism
- Escherichia coli (strain K12)
- Pharmacological action
- Unknown
- General Function
- Catalyzes the oxidation of D-lactate to pyruvate. Electrons derived from D-lactate oxidation are transferred to the ubiquinone/cytochrome electron transfer chain, where they may be used to provide energy for the active transport of a variety of amino acids and sugars across the membrane.
- Specific Function
- D-lactate dehydrogenase (quinone) activity
- Gene Name
- dld
- Uniprot ID
- P06149
- Uniprot Name
- D-lactate dehydrogenase
- Molecular Weight
- 64611.82 Da
References
- 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
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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
- Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF).
- Specific Function
- flavin adenine dinucleotide binding
- Gene Name
- glf
- Uniprot ID
- P37747
- Uniprot Name
- UDP-galactopyranose mutase
- Molecular Weight
- 42965.62 Da
References
- Kind
- Protein
- Organism
- Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
- Pharmacological action
- Unknown
- General 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 various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.
- Specific Function
- FAD binding
- Gene Name
- hmp
- Uniprot ID
- P39662
- Uniprot Name
- Flavohemoprotein
- Molecular Weight
- 44781.75 Da
References
- Kind
- Protein
- Organism
- Bacillus subtilis (strain 168)
- Pharmacological action
- Unknown
- General 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-methylglycine), N-ethylglycine and glycine (PubMed:11744710, PubMed:19864430, PubMed:9827558). Can also oxidize the herbicide glyphosate (N-phosphonomethylglycine) (PubMed:19864430). Displays lower activities on D-alanine, D-valine, D-proline and D-methionine (PubMed:11744710, PubMed:9827558). Does not act on L-amino acids and other D-amino acids (PubMed:9827558). Is essential for thiamine biosynthesis since the oxidation of glycine catalyzed by ThiO generates the glycine imine intermediate (dehydroglycine) required for the biosynthesis of the thiazole ring of thiamine pyrophosphate (PubMed:12627963).
- Specific Function
- FAD binding
- Gene Name
- thiO
- Uniprot ID
- O31616
- Uniprot Name
- Glycine oxidase
- Molecular Weight
- 40936.53 Da
References
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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
- Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon.
- Specific Function
- 1-pyrroline-5-carboxylate dehydrogenase activity
- Gene Name
- putA
- Uniprot ID
- P09546
- Uniprot Name
- Bifunctional protein PutA
- Molecular Weight
- 143813.665 Da
References
- Kind
- Protein
- Organism
- Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
- Pharmacological action
- Unknown
- General 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 adjacent bases on the same DNA strand upon exposure to ultraviolet radiation (By similarity).
- Specific Function
- deoxyribodipyrimidine photo-lyase activity
- Gene Name
- phr
- Uniprot ID
- P61497
- Uniprot Name
- Deoxyribodipyrimidine photo-lyase
- Molecular Weight
- 47900.455 Da
References
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- 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]
- 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
- Functions as an auxiliary enzyme in the beta-oxidation of unsaturated fatty acids with double bonds at even carbon positions. Catalyzes the NADPH-dependent reduction of the C4-C5 double bond of the acyl chain of 2,4-dienoyl-CoA to yield 2-trans-enoyl-CoA (PubMed:6363415, PubMed:9346310). Acts on both isomers, 2-trans,4-cis- and 2-trans,4-trans-decadienoyl-CoA, with almost equal efficiency (PubMed:6363415). Is not active with NADH instead of NADPH (PubMed:6363415). Does not show cis->trans isomerase activity (PubMed:10933894).
- Specific Function
- 2,4-dienoyl-CoA reductase (NADPH) activity
- Gene Name
- fadH
- Uniprot ID
- P42593
- Uniprot Name
- 2,4-dienoyl-CoA reductase [NADPH]
- Molecular Weight
- 72677.545 Da
References
- Kind
- Protein
- Organism
- Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
- Pharmacological action
- Unknown
- General Function
- Involved in aliphatic epoxide carboxylation (PubMed:10411892, PubMed:9150202). Catalyzes the reductive cleavage of the thioether bond of 2-oxopropyl-coenzyme M (2-KPC), and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M (PubMed:10411892).
- Specific Function
- 2-oxopropyl-CoM reductase (carboxylating) activity
- Gene Name
- xecC
- Uniprot ID
- Q56839
- Uniprot Name
- 2-oxopropyl-CoM reductase, carboxylating
- Molecular Weight
- 57347.19 Da
References
- Kind
- Protein
- Organism
- Shewanella frigidimarina
- Pharmacological action
- Unknown
- General Function
- Flavocytochrome that catalyzes the reduction of fumarate to succinate (PubMed:10978153). Is essential for fumarate respiration during anaerobic growth, acting as the terminal reductase (By similarity). Receives electrons from the membrane-bound tetraheme c-type cytochrome CymA (By similarity). In vitro, can use the artificial electron donor methyl viologen (PubMed:10978153).
- Specific Function
- electron transfer activity
- Gene Name
- fccA
- Uniprot ID
- P0C278
- Uniprot Name
- Fumarate reductase flavoprotein subunit
- Molecular Weight
- 60620.95 Da
References
- Kind
- Protein
- Organism
- Escherichia coli (strain K12)
- Pharmacological action
- Unknown
- General Function
- Not Available
- Specific Function
- flavin adenine dinucleotide binding
- Gene Name
- trxB
- Uniprot ID
- P0A9P4
- Uniprot Name
- Thioredoxin reductase
- Molecular Weight
- 34622.76 Da
References
- Kind
- Protein
- Organism
- Escherichia coli (strain K12)
- Pharmacological action
- Unknown
- General Function
- Catalyzes the NADH-dependent reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate (PubMed:9922232). Is required to provide the methyl group necessary for methionine synthetase to convert homocysteine to methionine; the methyl group is given by 5-methyltetrahydrofolate. Can also use NADPH as the reductant, but much less effectively than NADH (PubMed:9922232).
- Specific Function
- FAD binding
- Gene Name
- metF
- Uniprot ID
- P0AEZ1
- Uniprot Name
- 5,10-methylenetetrahydrofolate reductase
- Molecular Weight
- 33102.375 Da
References
- Kind
- Protein
- Organism
- Arthrobacter globiformis
- Pharmacological action
- Unknown
- General 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-methylenetetrahydrofolate through an unusual substrate channeling mechanism. This channeling occurs by nonbiased diffusion of the iminium intermediate through a large solvent cavity connecting active site 1 (N-terminus) and active site 2 (C-terminus). The synthesis of 5,10-methylenetetrahydrofolate (at active site 2) prevents the accumulation of formaldehyde, formed by hydrolysis of the iminium intermediate product (at active site 1). Does not oxidize sarcosine.
- Specific Function
- dimethylglycine oxidase activity
- 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
- Peroxidase whose active site is a redox-active cysteine-sulfenic acid.
- Specific Function
- flavin adenine dinucleotide binding
- 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
- Not Available
- Specific Function
- ferredoxin-NADP+ reductase activity
- 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
- 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. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.
- Specific Function
- flavin adenine dinucleotide binding
- 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
- Transports electrons between ferredoxin and NADPH.
- Specific Function
- ferredoxin-NADP+ reductase activity
- 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
- Has an optimum specificity for 4-carbon length fatty acyl-CoAs.
- Specific Function
- butyryl-CoA dehydrogenase activity
- 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
- Not Available
- Specific Function
- flavin adenine dinucleotide binding
- 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
- 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), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
- Specific Function
- dihydrolipoyl dehydrogenase activity
- 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
- Catalyzes the oxidation of the 1,2-dihydro- and 1,6-dihydro- isomeric forms of beta-NAD(P) back to beta-NAD(P)+. Has a preference for 1,2-dihydro-beta-NAD as substrate. May serve to protect primary metabolism dehydrogenases from inhibition by the 1,2-dihydro- and 1,6-dihydro-beta-NAD(P) isomers.
- Specific Function
- flavin adenine dinucleotide binding
- 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
- 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 adjacent bases on the same DNA strand upon exposure to ultraviolet radiation.
- Specific Function
- damaged DNA binding
- 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
- 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 adjacent bases on the same DNA strand upon exposure to ultraviolet radiation.
- Specific Function
- deoxyribodipyrimidine photo-lyase activity
- 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
- Catalyzes the oxidation of L-aspartate to iminoaspartate, the first step in the de novo biosynthesis of NAD(+) (PubMed:11294641, PubMed:2187483, PubMed:2841129, PubMed:7033218, PubMed:8706749, PubMed:8706750). Can use either oxygen or fumarate as electron acceptors, which allows the enzyme to be functional under aerobic and anaerobic conditions (PubMed:11294641, PubMed:12200425, PubMed:8706750). In vivo, fumarate is used under anaerobic conditions, and oxygen is the predominant electron acceptor under aerobic conditions due to the lower fumarate levels (PubMed:20149100). In vitro, fumarate is a more efficient electron acceptor and is kinetically superior to oxygen (PubMed:12200425, PubMed:20149100).
- Specific Function
- flavin adenine dinucleotide binding
- 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
- 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 circadian rhythm.
- Specific Function
- DNA binding
- 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
- 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
- Flavocytochrome that catalyzes the reduction of fumarate to succinate in vitro (PubMed:10455032). Is essentially unidirectional, catalyzing only fumarate reduction (PubMed:10455032). In vitro, can use the artificial electron donor methyl viologen (PubMed:10455032). May be involved in an alternative route for electron transport to Fe(3+) (PubMed:10455032).
- Specific Function
- FMN binding
- 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
- 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
- Not Available
- Specific Function
- D-arabinono-1,4-lactone oxidase activity
- 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
- 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
- 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
- Cell wall formation.
- Specific Function
- FAD binding
- 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
- 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
- Cell wall formation.
- Specific Function
- FAD binding
- 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
- 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 various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.
- Specific Function
- FAD binding
- Gene Name
- hmp
- Uniprot ID
- P24232
- Uniprot Name
- Flavohemoprotein
- Molecular Weight
- 43867.385 Da
- Kind
- Protein
- Organism
- Bacillus thermoglucosidasius
- Pharmacological action
- Unknown
- General Function
- Not Available
- Specific Function
- FMN binding
- 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
- Not Available
- Specific Function
- FAD binding
- 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
- The oxidation of camphor by cytochrome P450-CAM CamC requires the participation of the flavoprotein, putidaredoxin reductase CamA, and the iron-sulfur protein, putidaredoxin CamB, to mediate the transfer of electrons from NADH to P450 for oxygen activation.
- Specific Function
- flavin adenine dinucleotide binding
- 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
- flavin adenine dinucleotide binding
- 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
- 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 to 4-hydroxycrotonyl-CoA; (2) the hydroxyl group is substituted by a hydride derived from the now reduced FAD in an SN2' reaction leading to vinylacetyl-CoA; (3) isomerization to yield crotonyl-CoA.
- Specific Function
- 4 iron, 4 sulfur cluster binding
- 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
- Catalyzes the azurin dependent hydroxylation of the methyl group of 4-methylphenol to form 4-hydroxybenzaldehyde.
- Specific Function
- 4-cresol dehydrogenase (hydroxylating) activity
- 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
- 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 with the AhpC protein.
- Specific Function
- alkyl hydroperoxide reductase activity
- 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
- Not Available
- Specific Function
- dihydrolipoyl dehydrogenase activity
- 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
- Maintains high levels of reduced glutathione in the cytosol.
- Specific Function
- flavin adenine dinucleotide binding
- 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
- 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 phenylacetone as substrate, leading to the formation of benzyl acetate. Can also oxidize other aromatic ketones (benzylacetone, alpha-methylphenylacetone and 4-hydroxyacetophenone), some aliphatic ketones (dodecan-2-one and bicyclohept-2-en-6-one) and sulfides (e.g. methyl 4-tolylsulfide).
- Specific Function
- flavin adenine dinucleotide binding
- 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
- Electron transfer component of benzoate 1,2-dioxygenase system.
- Specific Function
- 2 iron, 2 sulfur cluster binding
- 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
- Not Available
- Specific Function
- flavin adenine dinucleotide binding
- 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
- Not Available
- Specific Function
- flavin adenine dinucleotide binding
- Gene Name
- fkbI
- Uniprot ID
- Q9KIE5
- Uniprot Name
- FkbI
- Molecular Weight
- 38183.945 Da
- Kind
- Protein
- Organism
- Pseudomonas putida
- Pharmacological action
- Unknown
- General 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 alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
- Specific Function
- dihydrolipoyl dehydrogenase activity
- 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
- 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 alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
- Specific Function
- dihydrolipoyl dehydrogenase activity
- 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
- 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 with the AhpC protein.
- Specific Function
- alkyl hydroperoxide reductase activity
- 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
- Not Available
- Specific Function
- ferredoxin-NADP+ reductase activity
- 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
- Transports electrons between flavodoxin or ferredoxin and NADPH (PubMed:12234497, PubMed:21306142, PubMed:8449868, PubMed:9839946). Reduces flavodoxin 1, flavodoxin 2 and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner (PubMed:12234497). Required for the activation of several enzymes such as pyruvate formate-lyase, anaerobic ribonucleotide reductase and cobalamin-dependent methionine synthase (PubMed:7042345, PubMed:8267617).
- Specific Function
- aconitate hydratase activity
- 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
- Catalyzes the oxidative decarboxylation of the C-terminal cysteine residue of mersacidin to an aminoenethiol residue.
- Specific Function
- FMN binding
- 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
- 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]
- 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]
- 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]
- 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 October 17, 2024 17:30