1 <h5>Introduction</h5> The hexokinase-catalysed phosphorylation of glucose by ATP occurs in all eukaryotic cells as the first step in the utilization of glucose, and the reaction is also widespread in prokaryotic cells; the subsequent steps vary, as the glucose 6-phosphate formed in the first step may have different metabolic fates in different types of cell and in different physiological conditions. Much information on hexokinases from different species has accumulated since the pioneering work of Meyerhof  on yeast hexokinase, and there are reviews on various aspects, including kinetics, structure, and genetics [2–9] . Glucose is the preferred substrate of the hexokinases, but they can also phosphorylate other hexoses to varying degrees, as recognized by the recommended name of hexokinase (ATP: d -hexose 6-phosphotransferase, EC 18.104.22.168). Only a few species, especially bacteria, are known to contain true glucokinases (ATP: d -glucose 6-phosphotransferase, EC 22.214.171.124), i.e., enzymes specific for glucose  . Hexokinases from different species differ in molecular mass and tissue distribution, and the enzyme often exists as a mixture of isoenzymes that differ in kinetic characteristics and molecular mass. In this review, we first give a broad picture of the general characteristics of the hexokinases in different phyla;
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research – Elsevier
Published: Mar 5, 1998
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