Determination of the Kinetic Constants of Glucose‐6‐phosphate 1‐Epimerase by Non‐Linear Optimization

Abstract

1 The overall kinetic constants of the reversible anomerisation of d‐glucopyranose 6‐phosphate from α to β 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 α to β and reverse are 0.0658 and 0.0389 s⁻¹, respectively. The Michaelis constants of the enzymic reaction are K^α_m 144 μM and K^β_m 55.5 μM with the turnover numbers of 1950 s⁻¹ and 446 s⁻¹ for the conversion of d‐glucopyranose 6‐phosphate from α to β and reverse, respectively.