Arginine N-succinyltransferase
| Arginine N-succinyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.109 | ||||||||
| CAS no. | 99676-48-9 | ||||||||
| 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 | ||||||||
| |||||||||
Arginine N-succinyltransferase (EC 2.3.1.109) is an enzyme that catalyzes the chemical reaction
-succinyl-L-arginine.svg.png)
The two substrates of this enzyme are arginine and succinyl-CoA. Its products are N(2)-succinyl-L-arginine and coenzyme A.[1][2][3] In this pathway, arginine is converted into breakdown products including ammonia, which is required for other processes in the bacteria.[4][5] The enzyme can also use ornithine as substrate and is involved in its catabolism in Pseudomonas aeruginosa.[6][7]
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.[8]
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code PDB: 1YLE.
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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ Enzyme 2.3.1.109 at KEGG Pathway Database.