Inhibition of Escherichia coliGlucosamine-6-phosphate Synthase by Reactive Intermediate Analogues
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چکیده
منابع مشابه
Inhibition of Escherichia coli Glucosamine-6-phosphate Synthase by Reactive Intermediate Analogues
Glucosamine-6-phosphate synthase (GlmS) catalyzes the formation of D-glucosamine 6-phosphate from D-fructose 6-phosphate using L-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. The most potent carbohydrate-based inhibitor...
متن کاملInhibition of Escherichia coli glucosamine-6-phosphate synthase by reactive intermediate analogues. The role of the 2-amino function in catalysis.
Glucosamine-6-phosphate synthase (GlmS) catalyzes the formation of D-glucosamine 6-phosphate from D-fructose 6-phosphate using L-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. The most potent carbohydrate-based inhibitor...
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INHIBITION OF HUMAN ERYTHROCYTE GLUCOSE 6-PHOSPHATE DEHYDROGENASE ACTIVITY BY DEHYDROEPIANDROSTERONE AND RELATED STEROIDS.
The inhibitory effects of several steroids on G6PD activity using intact erythrocytes are reported. Incubation of whole blood with dehydroepiandrosterone (DHEA) resulted in 42% and 12% inhibition in the enzyme activity in the presence and absence of oxygen, respectively. Addition of epinephrine and/or aminophylline into the incubation medium caused further enzyme inhibition suggesting a po...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2000
ISSN: 0021-9258
DOI: 10.1074/jbc.275.1.135