Purification and characterization of ribitol-5-phosphate and xylitol-5-phosphate dehydrogenases from strains of Lactobacillus casei.
A simple three-step procedure is described which yields electrophoretically homogeneous preparations of ribitol-5-phosphate dehydrogenase and xylitol-5-phosphate dehydrogenase. The former enzyme is a 115,000-molecular-weight protein composed of two subunits of identical size and is specific for its substrate, ribitol. The xylitol-5-phosphate dehydrogenase exists as a tetrameric protein with a molecular weight of 180,000; this enzyme oxidizes the phosphate esters of both xylitol and D-arabitol. Characterization of the physical, kinetic, and immunological properties of the two enzymes suggests that the functionally similar enzymes may not be structurally related.
D050542:D-Xylulose Reductase; D005779:Immunodiffusion; D007700:Kinetics; D007780:Lacticaseibacillus casei / Q000201:enzymology*; D008970:Molecular Weight; D012255:Ribitol / Q000378:metabolism; D013401:Sugar Alcohol Dehydrogenases / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D013402:Sugar Alcohols / Q000378:metabolism; D014993:Xylitol / Q000378:metabolism
D013402:Sugar Alcohols; D012255:Ribitol; D013401:Sugar Alcohol Dehydrogenases; C022529:ribitol 2-dehydrogenase; D050542:D-Xylulose Reductase; D014993:Xylitol; C014999:arabitol