IntEnz

EC 3.5.3.23 - N-succinylarginine dihydrolase

IntEnz Enzyme Nomenclature
EC 3.5.3.23

Names

Reaction

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

Comments:

Arginine, N2-acetylarginine and N2-glutamylarginine do not act as substrates [3]. This is the second enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.81 (succinylornithine transaminase), EC 1.2.1.71 (succinylglutamate semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase).

Links to other databases

References

1. Schneider, B.L., Kiupakis, A.K. and Reitzer, L.J.
   Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli.
   J. Bacteriol. 180 : 4278-4286 (1998). [PMID: 9696779]
2. Tocilj, A., Schrag, J. D., Li, Y., Schneider, B. L., Reitzer, L., Matte, A. and Cygler, M.
   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 : 15800-15808 (2005). [PMID: 15703173]
3. Vander Wauven, C. and Stalon, V.
   Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia.
   J. Bacteriol. 164 : 882-886 (1985). [PMID: 2865249]
4. Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V.
   Biosynthesis and metabolism of arginine in bacteria.
   Microbiol. Rev. 50 : 314-352 (1986). [PMID: 3534538]
5. Itoh, Y.
   Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa.
   J. Bacteriol. 179 : 7280-7290 (1997). [PMID: 9393691]

[EC 3.5.3.23 created 2006]