EC Tree |
3. Hydrolases |
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
3.5.1 In linear amides |
ID: | 3.5.1.97 |
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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; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.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 |
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 |
Title | Authors | Date | PubMed 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 CY | 2009 May 9 | 19426552 |
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 WJ | 2006 Mar | 16495538 |
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 LH | 2003 Feb | 12535081 |