@article{mbs:/content/journal/micro/10.1099/00221287-135-8-2163, author = "Witteveen, C. F. B. and Busink, R. and Van De Vondervoort, P. and Dijkema, C. and Swart, K. and Visser, J.", title = "l-Arabinose and d-Xylose Catabolism in Aspergillus niger", journal= "Microbiology", year = "1989", volume = "135", number = "8", pages = "2163-2171", doi = "https://doi.org/10.1099/00221287-135-8-2163", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-135-8-2163", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "A mutant of Aspergillus niger unable to grow on d-xylose and l-arabinose has been isolated. Genetic analysis revealed that the mutation is located on linkage group IV. Enzymic analysis revealed a deficiency in d-xylulose kinase activity. After transfer of growing mycelium to a medium containing either d-xylose or l-arabinose, the mutant accumulates large amounts of arabitol and xylitol, as shown by 13C NMR spectroscopy. These data and an analysis of enzyme activities induced by d-xylose and l-arabinose in the wild-type strain led to the following catabolic pathway for d-xylose: d-xylose - xylitol - d-xylulose - d-xylulose 5-phosphate; and for l-arabinose: l-arabinose - l-arabitol - l-xylulose - xylitol - d-xylulose - d-xylulose 5-phosphate. The reduction steps of the sugars to the corresponding polyols are all NADPH dependent. The oxidation steps of the polyols to the sugars are all NAD+ dependent. Fractionation of cell-free extracts gave information about the specificity of the enzymes and showed that all the reactions are catalysed by different enzymes.", }