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- W1545920123 abstract "Abstract Glucosamine-6-phosphate synthase (GlmS) catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate using glutamine as the ammonia source. Because N-acetylglucosamine is an essential building block of both bacterial cell walls and fungal cell wall chitin, the enzyme is a potential target for antibacterial and antifungal agents. N-Iodoacetylglucosamine 6-phosphate is an active site-directed irreversible inactivator of GlmS from Escherichia coli (k/K = 17 (±3) M s). Both fructose 6-phosphate and glutamine protect the enzyme from inactivation, indicating that this reagent is directed at both the sugar binding site and the glutamine binding site. Protection studies with fructose 6-phosphate demonstrate that the value of the dissociation constant for fructose 6-phosphate is 3.3 (±0.5) × 10M, approximately 3 orders of magnitude less than the K value for this substrate determined from initial velocity experiments (Badet, B., Vermoote, P., and Le Goffic, F.(1988) Biochemistry 27, 2282-2287)." @default.
- W1545920123 created "2016-06-24" @default.
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- W1545920123 date "1996-02-09" @default.
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- W1545920123 title "Active Site-directed Inactivation of Escherichia coli Glucosamine-6-phosphate Synthase DETERMINATION OF THE FRUCTOSE 6-PHOSPHATE BINDING CONSTANT USING A CARBOHYDRATE-BASED INACTIVATOR" @default.
- W1545920123 cites W1889077695 @default.
- W1545920123 doi "https://doi.org/10.1074/jbc.271.6.3052" @default.
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