(R)-amidase
From Wikipedia the free encyclopedia
| (R)-amidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.100 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
(R)-amidase (EC 3.5.1.100, R-stereospecific amidase, R-amidase) is an enzyme with systematic name (R)-piperazine-2-carboxamide amidohydrolase.[1] This enzyme catalyses the following chemical reaction
- (1) (R)-piperazine-2-carboxamide + H2O (R)-piperazine-2-carboxylic acid + NH3
- (2) beta-alaninamide + H2O beta-alanine + NH3
This enzyme also hydrolyses (R)-piperidine-3-carboxamide to (R)-piperidine-3-carboxylic acid and NH3.
References[edit]
- ^ Komeda H, Harada H, Washika S, Sakamoto T, Ueda M, Asano Y (April 2004). "A novel R-stereoselective amidase from Pseudomonas sp. MCI3434 acting on piperazine-2-tert-butylcarboxamide". European Journal of Biochemistry. 271 (8): 1580–90. CiteSeerX 10.1.1.547.2141. doi:10.1111/j.1432-1033.2004.04069.x. PMID 15066183.
External links[edit]
- (R)-amidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
