This article includes a list of general references, but it lacks sufficient corresponding inline citations. (April 2024) |
In enzymology, a glutamate N-acetyltransferase (EC 2.3.1.35) is an enzyme that catalyzes the chemical reaction
glutamate N-acetyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.3.1.35 | ||||||||
CAS no. | 37257-14-0 | ||||||||
Alt. names | ornithine transacetylase, alpha-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase, acetylglutamate synthetase, acetylglutamate-acetylornithine transacetylase, acetylglutamic synthetase, acetylglutamic-acetylornithine transacetylase, acetylornithinase, acetylornithine glutamate acetyltransferase, glutamate acetyltransferase, N-acetyl-L-glutamate synthetase, N-acetylglutamate synthase, N-acetylglutamate synthetase, ornithine acetyltransferase, 2-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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- N2-acetyl-L-ornithine + L-glutamate L-ornithine + N-acetyl-L-glutamate
Thus, the two substrates of this enzyme are N2-acetyl-L-ornithine and L-glutamate, whereas its two products are L-ornithine and N-acetyl-L-glutamate.
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 N2-acetyl-L-ornithine:L-glutamate N-acetyltransferase. This enzyme participates in the urea cycle and metabolism of amino groups.
Structural studies
editAs of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1VRA, 1VZ6, 1VZ7, and 1VZ8.
References
edit- Staub M, Denes G (1966). "Mechanism of arginine biosynthesis in Chlamydomonas reinhardti. I Purification and properties of ornithine acetyltransferase". Biochim. Biophys. Acta. 128 (1): 82–91. doi:10.1016/0926-6593(66)90144-5. PMID 5972370.