Glycine C-acetyltransferase
From Wikipedia, the free encyclopedia
In enzymology, a glycine C-acetyltransferase (EC 2.3.1.29) is an enzyme that catalyzes the chemical reaction:
- acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
Thus, the two substrates of this enzyme are acetyl-CoA and glycine, whereas its two products are CoA and 2-amino-3-oxobutanoate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:glycine C-acetyltransferase. Other names in common use include 2-amino-3-ketobutyrate CoA ligase, 2-amino-3-ketobutyrate coenzyme A ligase, 2-amino-3-ketobutyrate-CoA ligase, glycine acetyltransferase, and aminoacetone synthase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
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[edit] Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1FC4.
[edit] References
- IUBMB entry for 2.3.1.29
- BRENDA references for 2.3.1.29 (Recommended.)
- PubMed references for 2.3.1.29
- PubMed Central references for 2.3.1.29
- Google Scholar references for 2.3.1.29
- McGilvray D, Morris JG (1969). "Utilization of L-threonine by a species of Arthrobacter. A novel catabolic role for "aminoacetone synthase"". Biochem. J. 112: 657–71. PMID 5821726.
[edit] External links
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- The CAS registry number for this enzyme class is 37257-11-7.
[edit] Gene Ontology (GO) codes
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