GCAT

GCAT
Identifiers
Aliases	GCAT, KBL, glycine C-acetyltransferase
External IDs	OMIM: 607422 MGI: 1349389 HomoloGene: 8475 GeneCards: GCAT
Gene location (Human)
Chr.	Chromosome 22 (human)[1]
End	37,817,176 bp[1]
Gene ontology
Molecular function	• glycine C-acetyltransferase activity; • transferase activity; • pyridoxal phosphate binding; • transferase activity, transferring acyl groups; • catalytic activity;
Cellular component	• mitochondrion; • cell nucleus; • nucleoplasm; • nuclear speck; • mitochondrial inner membrane;
Biological process	• cellular amino acid metabolic process; • metabolism; • biosynthetic process; • threonine catabolic process; • L-threonine catabolic process to glycine;
	Sources:Amigo / QuickGO
Orthologs
	23464
	26912
	ENSG00000100116
	ENSMUSG00000006378
	O75600
	O88986
	NM_001171690; NM_014291
	NM_001161712; NM_013847
	NP_001165161; NP_055106
	NP_001155184; NP_038875
	Wikidata
View/Edit Human	View/Edit Mouse

Glycine C-acetyltransferase is a protein that in humans is encoded by the GCAT gene.[4]

Function

The degradation of L-threonine to glycine consists of a two-step biochemical pathway involving the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is first converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. This gene encodes the second enzyme in this pathway, which then catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The encoded enzyme is considered a class II pyridoxal-phosphate-dependent aminotransferase. Alternate splicing results in multiple transcript variants. A pseudogene of this gene is found on chromosome 14.

References

GRCh38: Ensembl release 89: ENSG00000100116 - Ensembl, May 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.
"Entrez Gene: Glycine C-acetyltransferase".

Jacquot C, Lanco X, Carbonnelle D, Sevestre O, Tomasoni C, Briad G, Juget M, Roussis V, Roussakis C (2002). "Effect of four genes (ALDH1, NRF1, JAM and KBL) on proliferation arrest in a non-small cell bronchopulmonary cancer line". Anticancer Research. 22 (4): 2229–35. PMID 12174908.
Tressel T, Thompson R, Zieske LR, Menendez MI, Davis L (Dec 1986). "Interaction between L-threonine dehydrogenase and aminoacetone synthetase and mechanism of aminoacetone production". The Journal of Biological Chemistry. 261 (35): 16428–37. PMID 3536927.
Edgar AJ, Polak JM (Mar 2000). "Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs". European Journal of Biochemistry / FEBS. 267 (6): 1805–12. doi:10.1046/j.1432-1327.2000.01175.x. PMID 10712613.
Hashizume, O., Ohnishi, S., Mito, T., Shimizu, A., Iashikawa, K., Nakada, K., ... & Hayashi, J. I. (2015). "Epigenetic regulation of the nuclear-coded GCAT and SHMT2 genes confers human age-associated mitochondrial respiration defects". Scientific Reports. 5 (10434). doi:10.1038/srep10434. PMC 5377050.CS1 maint: uses authors parameter (link)

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000100116 - Ensembl, May 2017

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

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

[entrez-4] "Entrez Gene: Glycine C-acetyltransferase".

GCAT

Function

References

Further reading