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. 1974 Nov;143(2):341–352. doi: 10.1042/bj1430341

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

Bruce D Burleigh Jr 1,*, Peter W J Rigby 1,†, Brian S Hartley 1,‡
PMCID: PMC1168389  PMID: 4376942

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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