3.1.1.45	4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate	-	-	
3.1.1.45	4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate	esterase activity on chromophoric ester substrate, p-nitrophenyl acetate and the synthetic active-site titrant, trans-cinnamoyl imidazole	94355	
3.1.1.45	4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate	mechanism	94355, 94356, 94357, 94358	
3.1.1.45	4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate	similar catalytic triads are found in alpha/beta hydrolase fold enzymes: DLH is the simplest one	94357, 94358, 94365	
3.1.1.45	4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate	the active-site Cys123 residue is part of a triad of residues consisting of Cys123, His202 and Asp171, and is reminiscent of the serine/cysteine proteases	94353, 94354, 94355, 94357, 94358, 94364	
3.1.1.45	4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate	the catalytic triad Cys123, His202 and Asp171 is a hybrid of the standard triads found in cysteine: Cys-His-Asn and serine: Ser-His-Asp proteases	94356, 94358	
3.1.1.45	4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate	wild-type enzyme catalytic triad: Cys-His-Asn, mutant enzyme catalytic triad: Ser-His-Asn	-, 650835