A single amino acid change (Y318F) in the L-arabitol dehydrogenase (LadA) from Aspergillus niger results in a significant increase in affinity for D-sorbitol |
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| Authors: | Lucy Rutten Cecile Ribot Blanca Trejo-Aguilar Han AB Wösten Ronald P de Vries |
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| Affiliation: | (1) Department of Crystal and Structural Chemistry, Utrecht University, 3584 Padualaan 8, CH Utrecht, the Netherlands;(2) Microbiology, Department of Biology, Utrecht University, 3584 Padualaan 8, CH Utrecht, the Netherlands;(3) Functional Genomics of Plant Pathogenic Fungi UMR 5240 CNRS-UCB-INSA-Bayer CropScience Microbiology, 14-20 Rue Pierre Baizet, B.P. 9163, 69263 Lyon cedex 09, France;(4) UMR BGPI, Equipe "Interactions riz-parasites", Campus International de Baillarguet, Montpellier, France;(5) Fungal Physiology, CBS Fungal Biodiversity Centre, 3584 Uppsalalaan 8, CT Utrecht, the Netherlands |
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| Abstract: | Background L-arabitol dehydrogenase (LAD) and xylitol dehydrogenase (XDH) are involved in the degradation of L-arabinose and D-xylose, which are among the most abundant monosaccharides on earth. Previous data demonstrated that LAD and XDH not only differ in the activity on their biological substrate, but also that only XDH has significant activity on D-sorbitol and may therefore be more closely related to D-sorbitol dehydrogenases (SDH). In this study we aimed to identify residues involved in the difference in substrate specificity. |
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