Jump to content

Glycine C-acetyltransferase

From Wikipedia, the free encyclopedia
glycine C-acetyltransferase
Identifiers
EC no.2.3.1.29
CAS no.37257-11-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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.

Structural studies

[edit]

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1FC4.

Human genes

[edit]

References

[edit]
  • McGilvray D, Morris JG (1969). "Utilization of L-threonine by a species of Arthrobacter. A novel catabolic role for "aminoacetone synthase"". Biochem. J. 112 (5): 657–71. doi:10.1042/bj1120657. PMC 1187769. PMID 5821726.