EC Number   |
Reaction |
Reference |
|---|
   3.1.1.81 | an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine |
- |
- |
| 3.1.1.81 | an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine |
active site structure and substrate binding, catalytic mechanism, overview |
666729 |
| 3.1.1.81 | an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine |
AiiA degrades AHLs in a tail length independent manner. The presence of the tail is required for activity. The putative oxyanion hole function of Y194 toward the substrate seem to show efficacy in stabilizing the intermediate state. Proton shuttling necessary for catalytic activity might be mediated by both water and substrate-based intra-molecular proton transfer |
730750 |
| 3.1.1.81 | an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine |
catalytic mechanism of the quorum-quenching metalloenzyme, overview |
690981 |
| 3.1.1.81 | an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine |
enzyme-substrate complex structure and detailed mechanism for the ring-opening hydrolysis of acyl homoserine lactone substrates as catalyzed by the AHL lactonase from Bacillus thuringiensis, overview |
690981 |
| 3.1.1.81 | an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine |
hydrolysis of the lactone ring |
-, 666264 |
| 3.1.1.81 | an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine |
reaction mechanism, and active site structure and function modeling, Asp108 residue, and not Tyr194, shuttles the proton during the reaction, overview |
692612 |
| 3.1.1.81 | an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine |
residues H106, D108, and H109, as well as H169 are important for catalytic activity |
665500 |
| 3.1.1.81 | an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine |
substrate binding and catalytic mecanism, overview |
666738 |
