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Glutamate N-acetyltransferase

glutamate N-acetyltransferase
Identifiers
EC no.2.3.1.35
CAS no.37257-14-0
Alt. namesornithine 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
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 glutamate N-acetyltransferase (EC 2.3.1.35) is an enzyme that catalyzes the chemical reaction

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

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1VRA, 1VZ6, 1VZ7, and 1VZ8.

References

  • 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.


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