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EC Number	Substrates	Commentary Substrates	Organism	Products	Commentary (Products)	Reversibility
3.1.1.25	2-coumaranone + H2O	25% of activity compared to L-pantoyl lactone	Agrobacterium tumefaciens	?	-	?
3.1.1.25	3,4-dihydrocoumarin + H2O	23% of activity compared to L-pantoyl lactone	Agrobacterium tumefaciens	?	-	?
3.1.1.25	L-pantoyl lactone + H2O	stereospecific hydrolysis	Agrobacterium tumefaciens	L-pantoic acid	-	?
3.1.1.25	2-coumaranone + H2O	25% of activity compared to L-pantoyl lactone	Agrobacterium tumefaciens AKU 316	?	-	?
3.1.1.25	3,4-dihydrocoumarin + H2O	23% of activity compared to L-pantoyl lactone	Agrobacterium tumefaciens AKU 316	?	-	?
3.1.1.25	L-pantoyl lactone + H2O	stereospecific hydrolysis	Agrobacterium tumefaciens AKU 316	L-pantoic acid	-	?
3.1.1.25	more	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	?	-	?
3.1.1.25	N-hexanoyl-(S)-homoserine lactone	-	Bacillus thuringiensis serovar kurstaki	N-hexanoyl-(S)-homoserine	-	?
3.1.1.25	N-hexanoyl-(S)-homoserine lactone	-	Bacillus thuringiensis serovar kurstaki 4A3	N-hexanoyl-(S)-homoserine	-	?
3.1.1.25	N-hexanoyl-(S)-homoserine lactone	-	Bacillus thuringiensis serovar kurstaki BGSC 4A3	N-hexanoyl-(S)-homoserine	-	?

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Release 2023.1 (January 2023)