Protein-coding gene in the species Homo sapiens
GCAT |
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Identifiers |
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Aliases | GCAT, KBL, glycine C-acetyltransferase |
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External IDs | OMIM: 607422; MGI: 1349389; HomoloGene: 8475; GeneCards: GCAT; OMA:GCAT - orthologs |
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RNA expression pattern |
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Bgee | Human | Mouse (ortholog) |
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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
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| | More reference expression data |
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BioGPS | |
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Gene ontology |
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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 |
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Orthologs |
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Species | Human | Mouse |
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Entrez | | |
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Ensembl | | |
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UniProt | | |
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RefSeq (mRNA) | | |
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RefSeq (protein) | | |
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Location (UCSC) | n/a | n/a |
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PubMed search | [1] | [2] |
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Wikidata |
View/Edit Human | View/Edit Mouse |
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Glycine C-acetyltransferase is a protein that in humans is encoded by the GCAT gene.[3]
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
- ^ "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".
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.