succinylglutamate desuccinylase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 3.5.1.96 | ||||||||
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 / QuickGO | ||||||||
|
In enzymology, a succinylglutamate desuccinylase (EC 3.5.1.96) is an enzyme that catalyzes the chemical reaction
- N-succinyl-L-glutamate + H2O succinate + L-glutamate
Thus, the two substrates of this enzyme are N-succinyl-L-glutamate and H2O, whereas its two products are succinate and L-glutamate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-succinyl-L-glutamate amidohydrolase. Other names in common use include N2-succinylglutamate desuccinylase, SGDS, and AstE. This enzyme participates in arginine and proline metabolism.
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. 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.
- Cunin R, Glansdorff N, Pierard A, Stalon V (1987). "Erratum report: Biosynthesis and metabolism of arginine in bacteria". Microbiol. Rev. 51 (1): 178. 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. PMC 107427. PMID 9696779.
Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
---|---|
3.5.1: Linear amides / Amidohydrolases | |
3.5.2: Cyclic amides/ Amidohydrolases | |
3.5.3: Linear amidines/ Ureohydrolases | |
3.5.4: Cyclic amidines/ Aminohydrolases | |
3.5.5: Nitriles/ Aminohydrolases | |
3.5.99: Other |
Enzymes | |
---|---|
Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
|
This EC 3.5 enzyme-related article is a stub. You can help Misplaced Pages by expanding it. |