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Literature summary for 3.1.1.25 extracted from

  • Charendoff, M.; Shah, H.; Briggs, J.
    New insights into the binding and catalytic mechanisms of Bacillus thuringiensis lactonase: insights into B. thuringiensis AiiA mechanism (2013), PLoS ONE, 8, e75395.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis P0CJ63 subsp. Kurstaki
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Reaction

Reaction Comment Organism Reaction ID
a 1,4-lactone + H2O = a 4-hydroxyacid upon substrate binding, the zinc-bridging hydroxide anion is effectively protected from re-protonation by the plug-like function of the acyl tails whereupon the ring-opening reaction can proceed. Subsequent protonation of the product's alkoxide group can then be accomplished by the intramolecular proton transfer from the intermediate state's carboxylic acid group where the resulting carboxylate group better accommodates the still-neighboring zinc ion Bacillus thuringiensis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme degrades acetylate homoserine lactones in a tail length independent manner, but the presence of the tail is required for activity. Residue Y194 seems to show efficacy in stabilizing the intermediate state. The proton shuttling necessary for catalytic activity might be mediated by both water and substrate-based intra-molecular proton transfer. Upon substrate binding, the zinc-bridging hydroxide anion is effectively protected from re-protonation by the plug-like function of the acyl tails whereupon the ring-opening reaction can proceed. Subsequent protonation of the product's alkoxide group can then be accomplished by the intramolecular proton transfer from the intermediate state's carboxylic acid group where the resulting carboxylate group better accommodates the still-neighboring zinc ion Bacillus thuringiensis ?
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Synonyms

Synonyms Comment Organism
AiiA
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 Bacillus thuringiensis