Penicillin amidase
| penicillin amidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.11 | ||||||||
| CAS no. | 9014-06-6 | ||||||||
| 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 penicillin amidase (EC 3.5.1.11) is an enzyme that catalyzes the chemical reaction
- penicillin + H2O a carboxylate + 6-aminopenicillanate
Thus, the two substrates of this enzyme are penicillin and H2O, whereas its two products are carboxylate and 6-aminopenicillanate.
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 penicillin amidohydrolase. Other names in common use include penicillin acylase, benzylpenicillin acylase, novozym 217, semacylase, alpha-acylamino-beta-lactam acylhydrolase, and ampicillin acylase. This enzyme participates in .
Structural studies[]
As of late 2007, 34 structures have been solved for this class of enzymes, with PDB accession codes 1AI4, 1AI5, 1AI6, 1AI7, 1AJN, 1AJP, 1AJQ, 1CP9, 1E3A, 1FXH, 1FXV, 1GK0, 1GK1, 1GK9, 1GKF, 1GM7, 1GM8, 1GM9, 1H2G, 1JX9, 1K5Q, 1K5S, 1K7D, 1KEC, 1PNK, 1PNL, 1PNM, 2ADV, 2AE3, 2AE4, 2AE5, 2IWM, 2PVA, and 3PVA.
References[]
- Sakaguchi K, Murao S (1950). "A preliminary report on a new enzyme, "penicillin-amidase"". J. Agric. Chem. Soc. Jpn. 23: 411.
- EC 3.5.1
- Enzymes of known structure
- EC 3.5 stubs