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

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

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 wi...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical journal Vol. 143; no. 2; pp. 341 - 352
Main Authors: Burleigh, B D, Rigby, P W, Hartley, B S
Format: Journal Article
Language:English
Published: England 01-11-1974
Subjects:
Alcohol Oxidoreductases - isolation & purification
Amino Acid Sequence
Amino Acids - analysis
Electrophoresis, Polyacrylamide Gel
Enzymology
Kinetics
Klebsiella - enzymology
Models, Chemical
Mutation
NAD - analysis
Ribose
Sulfhydryl Compounds - analysis
Xylitol
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Present address: Department of Biochemistry, The University of Texas M.D. Anderson Hospital and Tumor Institute, Texas Medical Center, Houston, Tex. 77025, U.S.A.
To whom reprint requests should be addressed, at the Department of Biochemistry, Imperial College, London SW7 2AZ, U.K.
Present address: Department of Biochemistry, Stanford University, Stanford, Calif. 94305, U.S.A.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj1430341