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.
Referencesedit
Schneider BL, Kiupakis AK, Reitzer LJ (1998). "Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli". J. Bacteriol. 180 (16): 4278–86. PMC107427. 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): 15800–8. 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): 882–6. PMC214334. PMID 2865249.
Cunin R, Glansdorff N, Pierard A, Stalon V (1986). "Biosynthesis and metabolism of arginine in bacteria". Microbiol. Rev. 50 (3): 314–52. PMC373073. 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): 7280–90. doi:10.1128/jb.179.23.7280-7290.1997. PMC179677. PMID 9393691.
succinylarginine, dihydrolase, enzymology, enzyme, that, catalyzes, chemical, reactionidentifiersec, 23databasesintenzintenz, viewbrendabrenda, entryexpasynicezyme, viewkeggkegg, entrymetacycmetabolic, pathwaypriamprofilepdb, structuresrcsb, pdbe, pdbsumgene, . In enzymology a N succinylarginine dihydrolase EC 3 5 3 23 is an enzyme that catalyzes the chemical reactionN succinylarginine dihydrolaseIdentifiersEC no 3 5 3 23DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumGene OntologyAmiGO QuickGOSearchPMCarticlesPubMedarticlesNCBIproteins N2 succinyl L arginine 2 H2O displaystyle rightleftharpoons N2 succinyl L ornithine 2 NH3 CO2Thus 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 editSchneider BL Kiupakis AK Reitzer LJ 1998 Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli J Bacteriol 180 16 4278 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 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 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 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 90 doi 10 1128 jb 179 23 7280 7290 1997 PMC 179677 PMID 9393691 Portal nbsp Biology This EC 3 5 enzyme related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title N succinylarginine dihydrolase amp oldid 1172354714, wikipedia, wiki, book, books, library,
