GLYAT

GLYAT
Identifikatori
Aliasi	GLYAT
Vanjski ID-jevi	OMIM: 607424 MGI: 2147502 HomoloGene: 64840 GeneCards: GLYAT
Lokacija gena (čovjek)
Hrom.	Hromosom 11 (čovjek)
Kraj	58,731,974 bp
Lokacija gena (miš)
Hrom.	Hromosom 19 (miš)
Kraj	12,631,275 bp
Obrazac RNK ekspresije
	; ;
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• aktivnost sa transferazom; • acyltransferase activity; • GO:0001948, GO:0016582 vezivanje za proteine; • glycine N-acyltransferase activity; • glycine N-benzoyltransferase activity;
Ćelijska komponenta	• mitochondrial matrix; • mitohondrija;
Biološki proces	• xenobiotic metabolic process; • acyl-CoA metabolic process; • monocarboxylic acid metabolic process; • response to toxic substance; • glycine metabolic process; • benzoyl-CoA metabolic process;
	Izvori:Amigo / QuickGO
Ortolozi
	10249
	107146
	ENSG00000149124
	ENSMUSG00000063683
	Q6IB77
	Q91XE0
	NM_201648; NM_005838
	NM_145935
	NP_005829; NP_964011
	NP_666047
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Glicin-N-aciltransferaza, znana i kao GLYAT, je enzim koji je kod ljudi kodiran genom GLYAT.^[5]^[6]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 296 aminokiselina, a molekulska težina Da. 33 924^[7]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MMLPLQGAQM	LQMLEKSLRK	SLPASLKVYG	TVFHINHGNP	FNLKAVVDKW
PDFNTVVVCP	QEQDMTDDLD	HYTNTYQIYS	KDPQNCQEFL	GSPELINWKQ
HLQIQSSQPS	LNEAIQNLAA	IKSFKVKQTQ	RILYMAAETA	KELTPFLLKS
KILSPNGGKP	KAINQEMFKL	SSMDVTHAHL	VNKFWHFGGN	ERSQRFIERC
IQTFPTCCLL	GPEGTPVCWD	LMDQTGEMRM	AGTLPEYRLH	GLVTYVIYSH
AQKLGKLGFP	VYSHVDYSNE	AMQKMSYTLQ	HVPIPRSWNQ	WNCVPL

Funkcija

Konjugati proteina glicin-N-aciltransferaze su glicin sa acil-CoA supstratima u mitohondrijama prvenstveno u jetri i bubrezima. Enzim glicin N-aciltransferaza uključen je u detoksikaciju širokog spektra ksenobiotika i endogenih metabolita. To uključuje benzoevu kiselinu, spoj koji se nalazi u voću i povrću i koristi se u medicini i prehrambenim proizvodima kao konzervans; salicilna kiselina, metabolit aspirina i nekoliko endogenih metabolita. Raznolikost se dokazuje širokim rasponom acilglicina koji se izlučuje urinom pacijenata s poremećajima metabolizma organskih kiselina. Još nije opisan nedostatak glicin N-aciltransferaze, ali je pokazano da postoje značajne međuindividualne varijacije u kapacitetu konjugacije glicina. Izoforma a-glicin N-aciltransferaze a je protein od 296 aminokiselina preveden iz prerađene varijante transkripta 1 iRNK. Kodiran je egzonima 2 do 6 transkripta iRNK.^[5]

Molekulska težina

U literaturi se navodi da je molekulska težina ovog spoja približno 30 kDa.^[6] ili približno 27 kDa.^[8] Predviđena veličina je 33,9 KDa. Za goveđi enzim prijavljen je raspon veličina između približno 33 kDa i oko 36 KDa (Nandi, 1979., Vessey, 1992., van der Westhuizen, 2000.). Predviđena veličina goveđeg GLYAT-a, na osnovu njegove sekvence (pristupni broj nm: 177486), je 33,9 kDa. Ovo se dobro slaže s eksperimentalno utvrđenim veličinama.^[8]^[9]^[10]

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000149124 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000063683 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b "Entrez Gene: GLYAT glycine-N-acyltransferase".
^ ^a ^b Mawal YR, Qureshi IA (decembar 1994). "Purification to homogeneity of mitochondrial acyl coa:glycine n-acyltransferase from human liver". Biochem. Biophys. Res. Commun. 205 (2): 1373–9. doi:10.1006/bbrc.1994.2817. PMID 7802672.
^ "UniProt, Q6IB77". Pristupljeno 22. 8. 2021.
^ ^a ^b van der Westhuizen FH, Pretorius PJ, Erasmus E (2000). "The utilization of alanine, glutamic acid, and serine as amino acid substrates for glycine N-acyltransferase". J. Biochem. Mol. Toxicol. 14 (2): 102–9. doi:10.1002/(SICI)1099-0461(2000)14:2<102::AID-JBT6>3.0.CO;2-H. PMID 10630424.
^ Nandi DL, Lucas SV, Webster LT (august 1979). "Benzoyl-coenzyme A:glycine N-acyltransferase and phenylacetyl-coenzyme A:glycine N-acyltransferase from bovine liver mitochondria. Purification and characterization". J. Biol. Chem. 254 (15): 7230–7. PMID 457678. Arhivirano s originala, 16. 11. 2007. Pristupljeno 22. 8. 2021.
^ Kelley M, Vessey DA (novembar 1992). "Structural comparison between the mitochondrial aralkyl-CoA and arylacetyl-CoA N-acyltransferases". Biochem. J. 288 (1): 315–7. doi:10.1042/bj2880315. PMC 1132116. PMID 1445276.

Dopunska literatura

Webster LT, Siddiqui UA, Lucas SV, et al. (1976). "Identification of separate acyl- CoA:glycine and acyl-CoA:L-glutamine N-acyltransferase activities in mitochondrial fractions from liver of rhesus monkey and man". J. Biol. Chem. 251 (11): 3352–8. PMID 931988.
Mawal YR, Qureshi IA (1994). "Purification to homogeneity of mitochondrial acyl coa:glycine n-acyltransferase from human liver". Biochem. Biophys. Res. Commun. 205 (2): 1373–9. doi:10.1006/bbrc.1994.2817. PMID 7802672.
Mawal YR, Qureshi IA (1995). "An immunodetection method for the quantitation of human acyl CoA:glycine N-acyltransferase in biological samples". Biochem. Mol. Biol. Int. 34 (3): 595–601. PMID 7833837.
Merkler DJ, Merkler KA, Stern W, Fleming FF (1996). "Fatty acid amide biosynthesis: a possible new role for peptidylglycine alpha-amidating enzyme and acyl-coenzyme A: glycine N-acyltransferase". Arch. Biochem. Biophys. 330 (2): 430–4. doi:10.1006/abbi.1996.0272. PMID 8660675.
Mawal Y, Paradis K, Qureshi IA (1997). "Developmental profile of mitochondrial glycine N-acyltransferase in human liver". J. Pediatr. 130 (6): 1003–7. doi:10.1016/S0022-3476(97)70293-2. PMID 9202629.
van der Westhuizen FH, Pretorius PJ, Erasmus E (2000). "The utilization of alanine, glutamic acid, and serine as amino acid substrates for glycine N-acyltransferase". J. Biochem. Mol. Toxicol. 14 (2): 102–9. doi:10.1002/(SICI)1099-0461(2000)14:2<102::AID-JBT6>3.0.CO;2-H. PMID 10630424.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
SCHACHTER D, TAGGART JV (2003). "Glycine N-acylase: purification and properties". J. Biol. Chem. 208 (1): 263–75. PMID 13174534.
Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.

Vanjski linkovi

GLYAT lokacija ljudskog genoma UCSC Genome Browser.

GLYAT human gene details in the UCSC Genome Browser.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000149124 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000063683 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: GLYAT glycine-N-acyltransferase".

[pmid7802672-6] Mawal YR, Qureshi IA (decembar 1994). "Purification to homogeneity of mitochondrial acyl coa:glycine n-acyltransferase from human liver". Biochem. Biophys. Res. Commun. 205 (2): 1373–9. doi:10.1006/bbrc.1994.2817. PMID 7802672.

[UniProt-7] "UniProt, Q6IB77". Pristupljeno 22. 8. 2021.

[pmid10630424-8] van der Westhuizen FH, Pretorius PJ, Erasmus E (2000). "The utilization of alanine, glutamic acid, and serine as amino acid substrates for glycine N-acyltransferase". J. Biochem. Mol. Toxicol. 14 (2): 102–9. doi:10.1002/(SICI)1099-0461(2000)14:2<102::AID-JBT6>3.0.CO;2-H. PMID 10630424.

[pmid457678-9] Nandi DL, Lucas SV, Webster LT (august 1979). "Benzoyl-coenzyme A:glycine N-acyltransferase and phenylacetyl-coenzyme A:glycine N-acyltransferase from bovine liver mitochondria. Purification and characterization". J. Biol. Chem. 254 (15): 7230–7. PMID 457678. Arhivirano s originala, 16. 11. 2007. Pristupljeno 22. 8. 2021.

[pmid1445276-10] Kelley M, Vessey DA (novembar 1992). "Structural comparison between the mitochondrial aralkyl-CoA and arylacetyl-CoA N-acyltransferases". Biochem. J. 288 (1): 315–7. doi:10.1042/bj2880315. PMC 1132116. PMID 1445276.

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p r u Enzimi
Teme	Aktivno mjesto Alosterna regulacija Difuzijski limitirani enzim EC broj Enzimska kataliza Inhibicija enzimskih reakcija Kinetika enzima Koenzim Kooperativnost Lineweaver–Burkov dijagram Michaelis–Mentenova kinetika Mjesto vezanja Spisak enzima
Tipovi	EC1 Oksidoreduktaze/spisak EC2 Transferaze/spisak EC3 Hidrolaze/spisak EC4 Lijaze/spisak EC5 Izomeraze/spisak EC6 Ligaze/spisak