Role of non-covalent enzyme‒substrate interactions in the reaction catalysed by cellobiose phosphorylase from Cellulomonas uda
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چکیده
منابع مشابه
Role of non-covalent enzyme-substrate interactions in the reaction catalysed by cellobiose phosphorylase from Cellulomonas uda.
Steady-state kinetic studies of the enzymic glucosyl transfer to and from phosphate catalysed by cellobiose phosphorylase from Cellulomonas uda have shown that this enzyme operates by a ternary-complex kinetic mechanism in which beta-cellobiose binds before phosphate, and beta-D-glucose and alpha-D-glucopyranosyl phosphate are released in that order. alpha-D-Glucopyranosyl fluoride (but not bet...
متن کاملCrystallization and X-ray diffraction studies of cellobiose phosphorylase from Cellulomonas uda.
Disaccharide phosphorylases are able to catalyze both the synthesis and the breakdown of disaccharides and have thus emerged as attractive platforms for tailor-made sugar synthesis. Cellobiose phosphorylase from Cellulomonas uda (CPCuda) is an enzyme that belongs to glycoside hydrolase family 94 and catalyzes the reversible breakdown of cellobiose [beta-D-glucopyranosyl-(1,4)-D-glucopyranose] t...
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15 صفحه اولEffects of end-product inhibition of Cellulomonas uda anaerobic growth on cellobiose chemostat culture.
Cellulomonas uda was grown anaerobically in a chemostat with 3.33 and 11.41 mM cellobiose in the feed medium at dilution rates varying from 0.017 to 0.29/h. Unusual results obtained were analyzed by using curves simulating the steady-state biomass. This unusual behavior could be accounted for by a classical growth model taking end-product inhibition into account. Acetate has been identified to ...
متن کاملStructural dissection of the reaction mechanism of cellobiose phosphorylase.
Cellobiose phosphorylase, a member of the glycoside hydrolase family 94, catalyses the reversible phosphorolysis of cellobiose into alpha-D-glucose 1-phosphate and D-glucose with inversion of the anomeric configuration. The substrate specificity and reaction mechanism of cellobiose phosphorylase from Cellvibrio gilvus have been investigated in detail. We have determined the crystal structure of...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2000
ISSN: 0264-6021
DOI: 10.1042/0264-6021:3510649