1887

Abstract

An NADPH-dependent L-xylulose reductase [xylitol:NADP 4-oxidoreductase; EC 1·1.1·10 (LXDH)] from was purified and characterized. It is an octamer with a monomeric molecular mass of 32 kDa, showing high specificity for L-xylulose, xylitol and NADP(H). The values for L-xylulose and xylitol are relatively high (16·5 and 925 mM, respectively). An NAD-dependent xylitol dehydrogenase [xylitol:NAD 2-oxidoreductase; EC 1·1.1·9 (DXDH)] was partially purified from the same fungus. It has a monomeric molecular mass of 40 kDa and shows a high specificity for D-xylulose, xylitol and NAD(H). The values for D-xylulose and xylitol are relatively low (approximately 4 and 50 mM, respectively). The reactivity towards xylitol, the product or substrate these enzymes have in common, confirms their role in the L-arabinose catabolic pathway.

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/content/journal/micro/10.1099/13500872-140-7-1679
1994-07-01
2021-08-05
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