N-succinylarginine dihydrolase

In enzymology, a N-succinylarginine dihydrolase (EC 3.5.3.23) is an enzyme that catalyzes the chemical reaction

N₂-succinyl-L-arginine + 2 H₂O N₂-succinyl-L-ornithine + 2 NH₃ + CO₂

Thus, the two substrates of this enzyme are N2-succinyl-L-arginine and H₂O, whereas its 3 products are N2-succinyl-L-ornithine, NH₃, and CO₂.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is N2-succinyl-L-arginine iminohydrolase (decarboxylating). Other names in common use include N2-succinylarginine dihydrolase, arginine succinylhydrolase, SADH, AruB, AstB, and 2-N-succinyl-L-arginine iminohydrolase (decarboxylating). This enzyme participates in arginine and proline metabolism.

References

• Schneider BL, Kiupakis AK, Reitzer LJ (1998). "Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli". J. Bacteriol. 180 (16): 4278&ndash, 86. PMC 107427. PMID 9696779.
• M; Schrag, JD; Li, Y; Schneider, BL; Reitzer, L; Matte, A; Cygler, M (2005). "Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli". J. Biol. Chem. 280 (16): 15800&ndash, 8. doi:10.1074/jbc.M413833200. PMID 15703173.
• Vander Wauven C, Stalon V (1985). "Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia". J. Bacteriol. 164 (2): 882&ndash, 6. 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&ndash, 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&ndash, 90. PMC 179677. PMID 9393691.