PMID: 12369908Oct 10, 2002Paper

Mechanism of action of D-xylose isomerase

Current Protein & Peptide Science
B Asbóth, G Náray-Szabó


The present knowledge on the stereochemical mechanism of action of glucose (or xylose) isomerase, one of the highest tonnage industrial enzymes, is summarized. First we deal shortly with experimental methods applied to study the structure and function of this enzyme: enzyme kinetics, protein engineering, X-ray crystallography, nuclear magnetic and electron paramagnetic resonance spectroscopy. Computational methods like homology modeling, molecular orbital, molecular dynamics and continuum electrostatic methods are also shortly treated. We discuss mostly those results and their contribution to the elucidation of the mechanism of action that have been published in the last decade. Structural characteristics of free xylose isomerase as well as its complexes with various ligands are depicted. This information provides a tool for the study of structural details of the enzyme mechanism. We present a general mechanism where the first step is ring opening, which is followed by the extension of the substrate to an open-chain conformation, a proton shuttle with the participation of a structural water molecule and the rate-determining hydride shift. The role of metal ions in the catalytic process is discussed in detail. Finally we present...Continue Reading


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