Mechanism of action of D-xylose isomerase

• Published in: Current protein & peptide science Vol. 1; no. 3; p. 237
• Main Authors: Asbóth, B, Náray-Szabó, G
• Format: Journal Article
• Language: English
• Published: United Arab Emirates 01-11-2000
• Subjects: Aldose-Ketose Isomerases - chemistry; Aldose-Ketose Isomerases - metabolism; Bacillus - enzymology; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Catalysis; Cations, Divalent - metabolism; Crystallography, X-Ray; Electron Spin Resonance Spectroscopy; Kinetics; Ligands; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Protons; Streptomyces - enzymology; Structure-Activity Relationship
• ISSN: 1389-2037
• DOI: 10.2174/1389203003381333

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 main trends in efforts of engineering the enzyme and delineate the prospective future lines. The review is completed by an extended bibliography with over 100 citations.