| N-acetylornithine carbamoyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.3.9 | ||||||||
| CAS no. | 890853-54-0 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a N-acetylornithine carbamoyltransferase (EC 2.1.3.9) is an enzyme that catalyzes the chemical reaction
- carbamoyl phosphate + N2-acetyl-L-ornithine phosphate + N-acetyl-L-citrulline
Thus, the two substrates of this enzyme are carbamoyl phosphate and N2-acetyl-L-ornithine, whereas its two products are phosphate and N-acetyl-L-citrulline.
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases. The systematic name of this enzyme class is carbamoyl-phosphate:N2-acetyl-L-ornithine carbamoyltransferase. Other names in common use include acetylornithine transcarbamylase, N-acetylornithine transcarbamylase, AOTC, and carbamoyl-phosphate:2-N-acetyl-L-ornithine carbamoyltransferase.
Structural studies[edit]
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 2G65, 2G68, 2G6A, and 2G6C.
References[edit]
- Shi D, Morizono H, Yu X, Roth L, Caldovic L, Allewell NM, Malamy MH, Tuchman M (April 2005). "Crystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several eubacteria". The Journal of Biological Chemistry. 280 (15): 14366–9. doi:10.1074/jbc.C500005200. PMID 15731101.
