GCAT

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

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] Band 22q13.1 Start 37,807,905 bp[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
Species	Human	Mouse
Entrez	23464	26912
Ensembl	ENSG00000100116	ENSMUSG00000006378
UniProt	O75600	O88986
RefSeq (mRNA)	NM_001171690 NM_014291	NM_001161712 NM_013847
RefSeq (protein)	NP_001165161 NP_055106	NP_001155184 NP_038875
Location (UCSC)	Chr 22: 37.81 – 37.82 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

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

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.
4. "Entrez Gene: Glycine C-acetyltransferase".

Further reading

• 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)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.