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. 1975 Jan 2;50(2):419-24.
doi: 10.1111/j.1432-1033.1975.tb09818.x.

Determination of the kinetic constants of glucose-6-phosphate 1-epimerase by non-linear optimization

Free article

Determination of the kinetic constants of glucose-6-phosphate 1-epimerase by non-linear optimization

E M Chance et al. Eur J Biochem. .
Free article

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.

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