Glutamate N-acetyltransferase
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
| glutamate N-acetyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.3.1.35 | ||||||||
| CAS number | 37257-14-0 | ||||||||
| 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 | ||||||||
| |||||||||
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. Other names in common use include 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, and 2-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase. This enzyme participates in 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.