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Succinylornithine transaminase

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succinylornithine transaminase
Identifiers
EC no.2.6.1.81
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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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.

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. 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. 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)