Acetylornithine transaminase
| Acetylornithine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.11 | ||||||||
| CAS no. | 9030-40-4 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Acetylornithine transaminase (EC 2.6.1.11) is an enzyme first characterised from Escherichia coli that catalyzes a reversible chemical reaction that is part of the biosynthesis of ornithine and arginine:[1][2]
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The two substrates of this enzyme in the forward direction shown are N(2)-acetyl-L-ornithine and α-ketoglutaric acid. Its products are N-acetyl-5-oxo-L-norvaline and L-glutamic acid. The enzyme has also been found in the genus Pseudomonas.[3][4]
This enzyme is a transferase, specifically a transaminase, which transfer nitrogenous groups. The systematic name of this enzyme class is N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase. Other names in common use include acetylornithine delta-transaminase, ACOAT, acetylornithine 5-aminotransferase, acetylornithine aminotransferase, N-acetylornithine aminotransferase, N-acetylornithine-delta-transaminase, N2-acetylornithine 5-transaminase, N2-acetyl-L-ornithine:2-oxoglutarate aminotransferase, succinylornithine aminotransferase, and 2-N-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase. It uses pyridoxal phosphate as a cofactor.[5]
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1VEF, PDB: 1WKG, PDB: 1WKH, PDB: 2E54, PDB: 2EH6, and PDB: 2ORD.
References
- ↑ Vogel HJ (1953). "Path of Ornithine Synthesis in Escherichia Coli". Proc. Natl. Acad. Sci. U.S.A. 39 (7): 578–83. Bibcode:1953PNAS...39..578V. doi:10.1073/pnas.39.7.578. PMC 1063827. PMID 16589307.
- ↑ Albrecht AM, Vogel HJ (1964). "Acetylornithine Delta-Transaminase. Partial Purification and Repression Behavior". J. Biol. Chem. 239: 1872–6. doi:10.1016/S0021-9258(18)91275-5. PMID 14213368.
- ↑ Voellmy R, Leisinger T (1975). "Dual role for N-2-acetylornithine 5-aminotransferase from Pseudomonas aeruginosa in arginine biosynthesis and arginine catabolism". J. Bacteriol. 122 (3): 799–809. doi:10.1128/JB.122.3.799-809.1975. PMC 246128. PMID 238949.
- ↑ Vander Wauven, C.; Stalon, V. (1985). "Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia". Journal of Bacteriology. 164 (2): 882–886. doi:10.1128/JB.164.2.882-886.1985. PMC 214334. PMID 2865249.
- ↑ Enzyme 2.6.1.11 at KEGG Pathway Database.