| succinylornithine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Succinylornithine transaminase homodimer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC no. | 2.6.1.81 | ||||||||
| 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 succinylornithine transaminase ( EC 2.6.1.81) is an enzyme that catalyzes the chemical reaction
- N2-succinyl-L-ornithine + 2-oxoglutarate N-succinyl-L-glutamate 5-semialdehyde + L-glutamate
Thus, the two substrates of this enzyme are N2-succinyl-L-ornithine and 2-oxoglutarate, whereas its two products are N-succinyl-L-glutamate 5-semialdehyde and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, 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. This enzyme participates in arginine and proline metabolism.
- Vander Wauven C, Stalon V (1985). "Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia". J. Bacteriol. 164 (2): 882–6. PMC 214334. PMID 2865249.
- Schneider BL, Kiupakis AK, Reitzer LJ (1998). "Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli". J. Bacteriol. 180 (16): 4278–86. 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. PMC 373073. PMID 3534538.
- 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.
- 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.
| succinylornithine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
|
Succinylornithine transaminase homodimer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC no. | 2.6.1.81 | ||||||||
| 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 succinylornithine transaminase ( EC 2.6.1.81) is an enzyme that catalyzes the chemical reaction
- N2-succinyl-L-ornithine + 2-oxoglutarate N-succinyl-L-glutamate 5-semialdehyde + L-glutamate
Thus, the two substrates of this enzyme are N2-succinyl-L-ornithine and 2-oxoglutarate, whereas its two products are N-succinyl-L-glutamate 5-semialdehyde and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, 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. This enzyme participates in arginine and proline metabolism.
- Vander Wauven C, Stalon V (1985). "Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia". J. Bacteriol. 164 (2): 882–6. PMC 214334. PMID 2865249.
- Schneider BL, Kiupakis AK, Reitzer LJ (1998). "Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli". J. Bacteriol. 180 (16): 4278–86. 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. PMC 373073. PMID 3534538.
- 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.
- 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.