RT Journal Article SR Electronic(1) A1 Witteveen, Cor F. B. A1 Weber, Frans A1 Busink, Ronald A1 Visser, JaapYR 1994 T1 Isolation and characterization of two xylitol dehydrogenases from Aspergillus niger JF Microbiology, VO 140 IS 7 SP 1679 OP 1685 DO https://doi.org/10.1099/13500872-140-7-1679 PB Microbiology Society, SN 1465-2080, AB An NADPH-dependent L-xylulose reductase [xylitol:NADP 4-oxidoreductase; EC 1·1.1·10 (LXDH)] from Aspergillus niger 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 K m 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 K m 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., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/13500872-140-7-1679