Determination of the kinetic constants of glucose-6-phosphate 1-epimerase by non-linear optimization.
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.
D000818:Animals; D002238:Carbohydrate Epimerases / Q000378:metabolism*; D002417:Cattle; D003201:Computers; D004926:Escherichia coli / Q000201:enzymology; D005958:Glucosephosphates; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008433:Mathematics; D008722:Methods; D010944:Plants / Q000201:enzymology; D012441:Saccharomyces cerevisiae; D013045:Species Specificity
D005958:Glucosephosphates; D002238:Carbohydrate Epimerases