Enzyme

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     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.1 In linear amides
ID:3.5.1.97
Description:Acyl-homoserine-lactone acylase.
Alternative Name: Quorum-quenching enzyme.
Quorum-quenching AHL acylase.
N-acyl-homoserine lactone acylase.
AHL-acylase.
Acyl-homoserine lactone acylase.
Cath: 1.10.1400.10; 1.10.439.10; 3.60.20.10; 2.30.120.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.97
BRENDA Enzyme Link: BRENDA 3.5.1.97
KEGG Enzyme Link: KEGG3.5.1.97
BioCyc Enzyme Link: BioCyc 3.5.1.97
ExPASy Enzyme Link: ExPASy3.5.1.97
EC2PDB Enzyme Link: EC2PDB 3.5.1.97
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.97
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.97
IntEnz Enzyme Link: IntEnz 3.5.1.97
MEDLINE Enzyme Link: MEDLINE 3.5.1.97
MSA:

3.5.1.97;

Phylogenetic Tree:

3.5.1.97;

Uniprot:
M-CSA:
RHEA:18937 an N-acyl-L-homoserine lactone + H2O = a carboxylate + L-homoserine lactone
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
A probable aculeacin A acylase from the Ralstonia solanacearum GMI1000 is N-acyl-homoserine lactone acylase with quorum-quenching activity.Chen CN, Chen CJ, Liao CT, Lee CY2009 May 919426552
Quorum quenching by an N-acyl-homoserine lactone acylase from Pseudomonas aeruginosa PAO1.Sio CF, Otten LG, Cool RH, Diggle SP, Braun PG, Bos R, Daykin M, Cámara M, Williams P, Quax WJ2006 Mar16495538
Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes.Lin YH, Xu JL, Hu J, Wang LH, Ong SL, Leadbetter JR, Zhang LH2003 Feb12535081