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Determination of the kinetic constants of glucose-6-phosphate 1-epimerase by non-linear optimization
European Journal of Biochemistry
|January 2, 1975
Abstract:
1. The overall kinetic constants of the reversible anomerisation of d-glucopyranose 6-phosphate from alpha to beta non-enzymatically as well as catalysed by glucose-6-phosphate 1-epimerase are determined by application of a novel computerized non-linear optimization technique. 2. The non-enzymic rate constants for the anomerisation of d-glucopyranose 6-phosphate from alpha to beta and reverse are 0.0658 and 0.0389s-minus 1, respectively. The Michaelis constants of the enzymic reaction are (see journal for formulas) with the turnover numbers of 1950s-minus 1 and 446s-minus 1 for the conversion of d-glucopyranose 6-phosphate from alpha to beta and reverse, respectively.