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

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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Hausman SZ,London J

doi

10.1128/jb.169.4.1651-1655.1987

subject

Has Abstract

pub_date

1987-04-01 00:00:00

pages

1651-5

issue

4

eissn

0021-9193

issn

1098-5530

journal_volume

169

pub_type

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