GCAT

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GCAT
Identifiers
AliasesGCAT, KBL, glycine C-acetyltransferase
External IDsMGI: 1349389 HomoloGene: 8475 GeneCards: GCAT
Gene location (Human)
Chromosome 22 (human)
Chr.Chromosome 22 (human)[1]
Chromosome 22 (human)
Genomic location for GCAT
Genomic location for GCAT
Band22q13.1Start37,807,905 bp[1]
End37,817,176 bp[1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

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

Function[edit]

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[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000100116 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:".
  3. ^ "Mouse PubMed Reference:".
  4. ^ "Entrez Gene: Glycine C-acetyltransferase".

Further reading[edit]

  • 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.

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