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- W1567646977 abstract "Abstract A constitutive stereospecific d-glucokinase was purified over 1000-fold from extracts of Aerobacter aerogenes PRL-R3. Only d-glucose (Km = 8 x 10-5 m and d-glucosamine (Ki = 4 x 10-4 m) were phosphorylated. The enzyme was inhibited by d-xylose (competitive with d-glucose, Ki = 3 x 10-3 m) but not by 34 other sugars and related compounds tested. It was inhibited by adenosine diphosphate (competitive with adenosine triphosphate, Ki = 4 x 10-4 m) but not by d-glucose 6-phosphate or d-mannose 6-phosphate. The pH optimum was 7.5 in glycylglycine buffer and about 8.9 in glycine buffer. Other properties studied were phosphoryl donor specificity, metal ion specificity, sedimentation coefficient, and stability. The product of d-glucose phosphorylation was identified as d-glucose 6-phosphate." @default.
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- W1567646977 date "1966-02-01" @default.
- W1567646977 modified "2023-09-30" @default.
- W1567646977 title "Stereospecific d-Glucokinase of Aerobacter aerogenes" @default.
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- W1567646977 doi "https://doi.org/10.1016/s0021-9258(18)96893-6" @default.
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