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- W2077893240 abstract "Tyr94 of Escherichia coli thymidylate synthase is thought to be involved, either directly or by activation of a water molecule, in the abstraction of a proton from C5 of the 2'-deoxyuridine 5'-monophosphate (dUMP) substrate. Mutation of Tyr94 leads to a 400-fold loss in catalytic activity. The structure of the Y94F mutant has been determined in the native state and as a ternary complex with thymidine 5'-monophosphate (dTMP) and 10-propargyl 5,8-dideazafolate (PDDF). There are no structural changes ascribable to the mutation other than loss of a water molecule hydrogen bonded to the tyrosine OH, which is consistent with a catalytic role for the phenolic OH." @default.
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- W2077893240 date "2006-08-18" @default.
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- W2077893240 title "Structure of the Y94F mutant of<i>Escherichia coli</i>thymidylate synthase" @default.
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- W2077893240 doi "https://doi.org/10.1107/s1744309106029691" @default.
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