PMID:1731613

Citation	Badet-Denisot, MA and Badet, B (1992) Chemical modification of glucosamine-6-phosphate synthase by diethyl pyrocarbonate: evidence of histidine requirement for enzymatic activity. Arch. Biochem. Biophys. 292:475-8
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.
Links	PubMed
Keywords	Binding Sites; Diethyl Pyrocarbonate/metabolism; Diethyl Pyrocarbonate/pharmacology; Escherichia coli/enzymology; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)/metabolism; Histidine; Kinetics; Protein Binding; Spectrophotometry, Ultraviolet; Sulfhydryl Compounds/analysis
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