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- W1981723997 abstract "Glucosamine-6-phosphate synthase from Escherichia coli was inactivated by diethylpyrocarbonate at pH 7.3 and 4 degrees C with a second-order rate constant of 1220 M-1 min-1. The difference spectrum of inactivated vs native enzyme had a maximum absorption at 242 nm, which is characteristic of N-carbethoxyhistidine. No trough at around 280 nm due to O-carbethoxytyrosine was observed and the sulfhydryl content of the enzyme was unchanged. Studies with [14C]diethylpyrocarbonate provided evidence that derivatization of a single histidine residue of the amino-terminal glutamine-binding domain inactivated glucosamine-6P synthase. These results are consistent with the participation of an histidine residue in a catalytic triad, Cys/His/Asp, necessary to generate ammonia from glutamine." @default.
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- W1981723997 date "1992-02-01" @default.
- W1981723997 modified "2023-09-25" @default.
- W1981723997 title "Chemical modification of glucosamine-6-phosphate synthase by diethyl pyrocarbonate: Evidence of histidine requirement for enzymatic activity" @default.
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- W1981723997 doi "https://doi.org/10.1016/0003-9861(92)90018-r" @default.
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