Biology:Arginine N-succinyltransferase
| arginine N-succinyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.3.1.109 | ||||||||
| CAS number | 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 | ||||||||
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In enzymology, an arginine N-succinyltransferase (EC 2.3.1.109) is an enzyme that catalyzes the chemical reaction
- succinyl-CoA + L-arginine [math]\displaystyle{ \rightleftharpoons }[/math] 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
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1YLE.
References
Further reading
- "N2-succinylornithine in ornithine catabolism of Pseudomonas aeruginosa". Arch. Microbiol. 150 (4): 400–4. 1988. doi:10.1007/BF00408314. PMID 3144259.
- "Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia". J. Bacteriol. 164 (2): 882–6. 1985. doi:10.1128/JB.164.2.882-886.1985. PMID 2865249.
- "Purification and properties of a succinyltransferase from Pseudomonas aeruginosa specific for both arginine and ornithine". Eur. J. Biochem. 224 (3): 853–61. 1994. 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. PMID 9393691.
- "Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli". J. Bacteriol. 180 (16): 4278–86. 1998. doi:10.1128/JB.180.16.4278-4286.1998. PMID 9696779.
- "Biosynthesis and metabolism of arginine in bacteria". Microbiol. Rev. 50 (3): 314–52. 1986. doi:10.1128/MMBR.50.3.314-352.1986. PMID 3534538.
- "Erratum report: Biosynthesis and metabolism of arginine in bacteria". Microbiol. Rev. 51 (1): 178. 1987. PMID 16350242.
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