In enzymology, an arginine N-succinyltransferase (EC 2.3.1.109) is an enzyme that catalyzes the chemical reaction
| arginine N-succinyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.109 | ||||||||
| CAS no. | 99676-48-9 | ||||||||
| 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 | ||||||||
| |||||||||
- succinyl-CoA + L-arginine CoA + N2-succinyl-L-arginine
Thus, the two substrates of this enzyme are succinyl-CoA and L-arginine, whereas its two products are CoA and N2-succinyl-L-arginine.[1]
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is succinyl-CoA:L-arginine N2-succinyltransferase. Other names in common use include arginine succinyltransferase, AstA, arginine and ornithine N2-succinyltransferase, AOST, AST, and succinyl-CoA:L-arginine 2-N-succinyltransferase. This enzyme participates in arginine and proline metabolism.
Structural studies
editAs of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1YLE.
References
editFurther reading
edit- Vander Wauven C, Jann A, Haas D, Leisinger T, Stalon V (1988). "N2-succinylornithine in ornithine catabolism of Pseudomonas aeruginosa". Arch. Microbiol. 150 (4): 400–4. doi:10.1007/BF00408314. PMID 3144259. S2CID 12934236.
- 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.
- Tricot C, Vander Wauven C, Wattiez R, Falmagne P, Stalon V (1994). "Purification and properties of a succinyltransferase from Pseudomonas aeruginosa specific for both arginine and ornithine". Eur. J. Biochem. 224 (3): 853–61. doi:10.1111/j.1432-1033.1994.00853.x. PMID 7523119.
- 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/MMBR.50.3.314-352.1986. PMC 373073. PMID 3534538.
- Cunin R, Glansdorff N, Pierard A, Stalon V (1987). "Erratum report: Biosynthesis and metabolism of arginine in bacteria". Microbiol. Rev. 51 (1): 178. doi:10.1128/mr.51.1.178-178b.1987. PMC 373097. PMID 16350242.
