Abstract
18O exchange between the glucosyl and phosphoryl bridge oxygens of glucose-1-P with potato starch phosphorylase in the presence of cyclodextrins suggests that glycogen phosphorylases catalyze a double displacement reaction with retention of configuration involving a glucosyl-enzyme-intermediate (Ref. 1). In the framework of this catalytic mechanism and based on recent information on the three-dimensional structure of muscle glycogen phosphorylase (Ref. 2, 3), a possible role of the phosphate group of pyridoxal-5′-P either as proton- or as glucosyl-donor-acceptor group is discussed:
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