L-proline amide hydrolase
L-proline amide hydrolase (EC 3.5.1.101, S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase, LaaA, L-amino acid amidase) is an enzyme with systematic name (S)-piperidine-2-carboxamide amidohydrolase.[1] This enzyme catalyses the following chemical reaction
- (1) (S)-piperidine-2-carboxamide + H2O (S)-piperidine-2-carboxylic acid + NH3
- (2) L-prolinamide + H2O L-proline + NH3
| L-proline amide hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.1.101 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
References
- Komeda H, Harada H, Washika S, Sakamoto T, Ueda M, Asano Y (April 2004). "S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase from Pseudomonas azotoformans IAM 1603 is a novel L-amino acid amidase". European Journal of Biochemistry. 271 (8): 1465–75. doi:10.1111/j.1432-1033.2004.04056.x. PMID 15066172.
External links
- L-proline+amide+hydrolase at the US National Library of Medicine Medical Subject Headings (MeSH)
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