N-succinylarginine dihydrolase

N-succinylarginine dihydrolase
Identifiers
EC number	3.5.3.23
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 / EGO
Search PMC articles PubMed articles

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 $\rightleftharpoons$ 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): 4278–86. PMC 107427. PMID 9696779. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=107427. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=214334. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=373073. 
• 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. PMC 179677. PMID 9393691. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=179677. 

This hydrolase article is a stub. You can help Wikipedia by expanding it.v · Categories: Hydrolase stubs EC 3.5.3 Enzymes of unknown structure Wikimedia Foundation. 2010. Игры ⚽ Поможем решить контрольную работу N-substituted formamide deformylase The News Herald Look at other dictionaries: Hydrolase — Cristal de lysozyme Les hydrolases constituent une classe d enzymes qui catalysent les réactions d hydrolyse de molécules suivant la réaction générale : R R + H2O ⇌ R OH + R H On y trouve par exemple les estérases, qui hydrolysent les …   Wikipédia en Français EC 3.5 — Le groupe EC3.5 rassemble des enzymes appartenant à la famille des hydrolases. Elles ont pour particularité de catalyser des réactions d hydrolyse dans des molécules possédant un carbone et un azote liés par liaison simple, double ou triple. À la …   Wikipédia en Français 18+ © Academic, 2000-2024 Contact us: Technical Support, Advertising Dictionaries export, created on PHP, Joomla, Drupal, WordPress, MODx. Mark and share Search through all dictionaries Translate… Search Internet Share the article and excerpts Direct link … Do a right-click on the link above and select “Copy Link”