1887

Abstract

Extracts of grown aerobically on xylose contained xylitol dehydrogenase and -xylose reductase activities. Extracts of cells grown on glucose contained one-tenth as much xylose reductase and no detectable xylitol dehydrogenase. The xylitol dehydrogenase was purified to near homogeneity, and is a tetramer of 45 kDa subunits. This labile enzyme, could be stabilized by glycerol (25%) and was rapidly inactivated by 10 m-EDTA. It catalyses the reversible, NAD-dependent oxidation of xylitol to xylulose. Apparent values are 19 m-xylitol and 0·3 m-NAD at 30 °C, pH 8·5. Partially purified preparations of xylose reductase catalysed the NADPH-dependent reduction of -xylose to xylitol, and were 16 times as active with 33 m--glyceraldehyde as with 33 m--xylose. Apparently grown on xylose has the necessary enzymes to convert xylose to xylulose by the oxidoreductive pathway.

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1989-06-01
2024-12-02
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