EC number:3.5.1.11

Enzyme

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EC Tree
     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.1 In linear amides
ID:3.5.1.11
Description:Penicillin amidase.
Alternative Name: Penicillin acylase.
Cath: 1.10.10.2120; 1.10.1400.10; 1.10.287.150; 1.10.439.10; 3.60.20.10; 3.60.60.10; 2.30.120.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.11
BRENDA Enzyme Link: BRENDA 3.5.1.11
KEGG Enzyme Link: KEGG3.5.1.11
BioCyc Enzyme Link: BioCyc 3.5.1.11
ExPASy Enzyme Link: ExPASy3.5.1.11
EC2PDB Enzyme Link: EC2PDB 3.5.1.11
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.11
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.11
IntEnz Enzyme Link: IntEnz 3.5.1.11
MEDLINE Enzyme Link: MEDLINE 3.5.1.11

EC number:3.5.1.11

MSA:

3.5.1.11;
Phylogenetic Tree:

3.5.1.11;
Uniprot:
M-CSA:
RHEA:18693 H2O + penicillin = 6-aminopenicillanate + a carboxylate
RULE(radius=1) [*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:6].[*:5]-[NH2;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Penicillin acylase has a single-amino-acid catalytic centre.Duggleby HJ, Tolley SP, Hill CP, Dodson EJ, Dodson G, Moody PC1995 Jan 197816145
Structural and kinetic studies on ligand binding in wild-type and active-site mutants of penicillin acylase.Alkema WB, Hensgens CM, Snijder HJ, Keizer E, Dijkstra BW, Janssen DB2004 May15254299
Crystal structures of penicillin acylase enzyme-substrate complexes: structural insights into the catalytic mechanism.McVey CE, Walsh MA, Dodson GG, Wilson KS, Brannigan JA2001 Oct 1211601852
Penicillin V acylase crystal structure reveals new Ntn-hydrolase family members.Suresh CG, Pundle AV, SivaRaman H, Rao KN, Brannigan JA, McVey CE, Verma CS, Dauter Z, Dodson EJ, Dodson GG1999 May10331865