GCAT

GCAT
Identifiers
Aliases	GCAT, KBL, glycine C-acetyltransferase
External IDs	OMIM: 607422; MGI: 1349389; HomoloGene: 8475; GeneCards: GCAT; OMA:GCAT - orthologs
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas right lobe of liver left ventricle oocyte endothelial cell prefrontal cortex Brodmann area 9 amygdala nucleus accumbens cingulate gyrus n/a More reference expression data BioGPS n/a
Gene ontology Molecular function glycine C-acetyltransferase activity transferase activity pyridoxal phosphate binding acyltransferase activity catalytic activity Cellular component mitochondrion nucleus nucleoplasm nuclear speck mitochondrial inner membrane Biological process cellular amino acid metabolic process metabolism biosynthesis threonine catabolic process L-threonine catabolic process to glycine Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23464 26912 Ensembl n/a 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) n/a n/a PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

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.

GCAT can also be used to refer to Grace Cat, who goes by the nickname of GCAT.

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. doi:10.1016/S0021-9258(18)66584-6. 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. 267 (6): 1805–12. doi:10.1046/j.1432-1327.2000.01175.x. PMID 10712613.
• Hashizume O, Ohnishi S, Mito T, Shimizu A, Ishikawa K, Nakada K, Soda M, Mano H, Togayachi S, Miyoshi H, Okita K, Hayashi J (2015). "Epigenetic regulation of the nuclear-coded GCAT and SHMT2 genes confers human age-associated mitochondrial respiration defects". Scientific Reports. 5 (10434): 10434. Bibcode:2015NatSR...510434H. doi:10.1038/srep10434. PMC 5377050. PMID 26000717.

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