Enzyme
glutamate N -acetyltransferase 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 IntEnz IntEnz view BRENDA BRENDA entry ExPASy NiceZyme view KEGG KEGG entry MetaCyc metabolic pathway PRIAM profile PDB structuresRCSB PDB PDBe PDBsum Gene Ontology AmiGO / QuickGO
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
⇌ ⇌ -->
{\displaystyle \rightleftharpoons }
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 .
Activity Regulation Classification Kinetics Types