Purification and characterization of ribitol-5-phosphate and xylitol-5-phosphate dehydrogenases from strains of Lactobacillus casei

J Bacteriol. 1987 Apr;169(4):1651-5. doi: 10.1128/jb.169.4.1651-1655.1987.

Abstract

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.

MeSH terms

  • D-Xylulose Reductase
  • Immunodiffusion
  • Kinetics
  • Lactobacillus casei / enzymology*
  • Molecular Weight
  • Ribitol / metabolism
  • Sugar Alcohol Dehydrogenases / immunology
  • Sugar Alcohol Dehydrogenases / isolation & purification*
  • Sugar Alcohol Dehydrogenases / metabolism
  • Sugar Alcohols / metabolism
  • Xylitol / metabolism

Substances

  • Sugar Alcohols
  • Ribitol
  • Sugar Alcohol Dehydrogenases
  • ribitol 2-dehydrogenase
  • D-Xylulose Reductase
  • Xylitol
  • arabitol