GCAT

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.


This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.