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- W2034971990 abstract "A designed single amino acid substitution can alter the catalytic activity and mechanism of 4-oxalocrotonate tautomerase (4-OT). While the wild-type enzyme catalyzes only the tautomerization of oxalocrotonate, the Pro1Ala mutant (P1A) catalyzes two reactions--the original tautomerization reaction and the decarboxylation of oxaloacetate. Although the N-terminal amine group of P1A is involved in both reactions, our results support a nucleophilic mechanism for the decarboxylase activity, in contrast to the general acid/base mechanism that has been previously established for the tautomerase activity. These findings demonstrate that a single catalytic group in a 4-OT mutant can catalyze two reactions by two different mechanisms." @default.
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- W2034971990 date "2002-09-02" @default.
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- W2034971990 title "Mutants of 4-Oxalocrotonate Tautomerase Catalyze the Decarboxylation of Oxaloacetate through an Imine Mechanism" @default.
- W2034971990 doi "https://doi.org/10.1002/1439-7633(20020902)3:9<845::aid-cbic845>3.0.co;2-2" @default.
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