Succinylornithine transaminase
| Succinylornithine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Succinylornithine transaminase homodimer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC no. | 2.6.1.81 | ||||||||
| 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 | ||||||||
| |||||||||
Succinylornithine transaminase (EC 2.6.1.81) is a pyridoxal phosphate-dependent enzyme that catalyzes the chemical reaction
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The two substrates of this enzyme first characterised from Pseudomonas cepacia are N2-succinyl-L-ornithine (1) and α-ketoglutaric acid. Its products are N-succinyl-L-glutamate 5-semialdehyde (2) and L-glutamic acid. In this bacterium, the reaction is part of the breakdown pathway of the amino acid arginine.[1] The enzyme has also been found in Pseudomonas aeruginosa[2] and Escherichia coli.[3][4][5]
This enzyme is a transferase, specifically a transaminase, which transfer nitrogenous groups. The systematic name of this enzyme class is N2-succinyl-L-ornithine:2-oxoglutarate 5-aminotransferase. Other names in common use include succinylornithine aminotransferase, N2-succinylornithine 5-aminotransferase, AstC, SOAT, and 2-N-succinyl-L-ornithine:2-oxoglutarate 5-aminotransferase. It participates in arginine and proline metabolism.[6]
References
- ↑ Vander Wauven C, Stalon V (1985). "Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia". J. Bacteriol. 164 (2): 882–6. doi:10.1128/jb.164.2.882-886.1985. PMC 214334. PMID 2865249.
- ↑ Itoh Y (1997). "Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa". J. Bacteriol. 179 (23): 7280–90. doi:10.1128/jb.179.23.7280-7290.1997. PMC 179677. PMID 9393691.
- ↑ Schneider BL, Kiupakis AK, Reitzer LJ (1998). "Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli". J. Bacteriol. 180 (16): 4278–86. doi:10.1128/JB.180.16.4278-4286.1998. PMC 107427. PMID 9696779.
- ↑ Cunin R, Glansdorff N, Pierard A, Stalon V (1986). "Biosynthesis and metabolism of arginine in bacteria". Microbiol. Rev. 50 (3): 314–52. doi:10.1128/mr.50.3.314-352.1986. PMC 373073. PMID 3534538.
- ↑ Stalon V, Vander Wauven C, Momin P, Legrain C (1987). "Catabolism of arginine, citrulline and ornithine by Pseudomonas and related bacteria". J. Gen. Microbiol. 133 (9): 2487–95. doi:10.1099/00221287-133-9-2487. PMID 3129535.
- ↑ Enzyme 2.6.1.81 at KEGG Pathway Database.