A comparison of wild-type and mutant ribitol dehydrogenases from Klebsiella aerogenes.

The Biochemical journal ·Vol. 143 ·No. 2 ·1974-11-00 ·Pages 341-52

Burleigh BD, Rigby PW, Hartley BS

Abstract

A ribitol dehydrogenase (ribitol-NAD(+) oxidoreductase, EC. 1.1.1.56) having increased specificity and catalytic efficiency toward xylitol was isolated from mutant strains of Klebsiella aerogenes, which were selected for increased growth rate on xylitol over the ribitol dehydrogenase constitutive wild-type organism. 2. The mutant enzyme was purified to homogeneity and its general characteristics were compared with those of the previously purified wild-type enzyme. 3. Initial-velocity steady-state kinetic parameters were determined for both wild-type and mutant enzymes and the results compared. 4. The results are interpreted in terms of a model in which the mutant enzyme results from a small change of amino acid sequence, which affects both the stability and conformational equilibria of the molecule.

MeSH Terms

Alcohol Oxidoreductases/isolation & purification Amino Acid Sequence Amino Acids/analysis Electrophoresis, Polyacrylamide Gel Kinetics Klebsiella/enzymology Models, Chemical Mutation NAD/analysis Ribose Sulfhydryl Compounds/analysis Xylitol

Chemicals

Amino Acids Sulfhydryl Compounds NAD Ribose Alcohol Oxidoreductases Xylitol

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Burleigh B D

Rigby P W

Hartley B S

References (13)

13 references, click to expand

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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1430341

Published

1974-11-00

Pages

341-52

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1168389

Subset

External Links

PubMed source DOI: 10.1042/bj1430341 PMC Full Text View journal details

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A comparison of wild-type and mutant ribitol dehydrogenases from Klebsiella aerogenes.

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