The stereochemical course of phosphoryl transfer catalysed by glucokinase.
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چکیده
منابع مشابه
The stereochemical course of phosphoryl transfer catalysed by glucokinase.
Adenosine 5'-[gamma(S)-16O,17O,18O]triphosphate has been used to determine the stereo-chemical course of phosphoryl transfer catalysed by rat liver glucokinase. The chirality of the product, D-glucose 6-[16O,17O,18O]phosphate was analysed by 31P n.m.r. spectroscopy. The reaction proceeds with inversion of configuration at phosphorus. The simplest interpretation of this result, which is the same...
متن کاملThe stereochemical course of phosphoryl transfer catalysed by glucose 6-phosphatase.
Rat liver microsomal glucose 6-phosphatase catalyses phosphoryl transfer between D-glucose 6-[(R)-16O,17O,18O]phosphate and D-glucose with retention of configuration at the phosphorus atom. Since individual phosphoryl-transfer steps appear in general to occur with inversion of configuration, this observation is most simply interpreted in terms of a double-displacement mechanism with a phosphory...
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Phenyl [(R)-16O,17O,18O]sulphate was synthesized and used to study the stereochemical course of sulphuryl transfer to p-cresol catalysed by arylsulphatase II from Aspergillus oryzae. The reaction was shown to proceed with retention of configuration at the sulphur atom, providing evidence for the involvement of a sulpho-enzyme intermediate on the reaction pathway.
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متن کاملA stereochemical investigation of phosphoryl transfer catalysed by phosphoglucomutase by the use of a - D - glucose 1 - [ ( S ) - 60 , 170 , 180 jphosphate
Rabbit muscle phosphoglucomutase converts a-D-glucose 1_[(S)-160,17O,8Olphosphate into D-glucose 6-[160,'70,18Olphosphate, which is shown by 31P n.m.r. spectroscopy, after cyclization and methylation, to have the (S)-configuration at the phosphorus atom. Since phosphoglucomutase is known to catalyse phosphoryl transfer by way of a phospho-enzyme intermediate, and since individual phosphoryl-tra...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1982
ISSN: 0264-6021
DOI: 10.1042/bj2010421