Characterisation of a secondary alcohol dehydrogenase from Xanthomonas campestris DSM 3586

The chromosomal locus NP_636946 of Xanthomonas campestris DSM 3586 (ATCC 33913) which was earlier presumed to encode a quinoprotein glucose dehydrogenase has been cloned, expressed in Escherichia coli and the recombinant enzyme has been characterised. It was found to have no glucose dehydrogenase ac...

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Bibliographic Details
Published in:Applied microbiology and biotechnology 2005-03, Vol.66 (6), p.664-667
Main Authors: SALUSJÄRVI, Tuomas, HVORSLEV, Niels, MIASNIKOV, Andrei N
Format: Article
Language:English
Subjects:
Alcohol Oxidoreductases - genetics
Alcohol Oxidoreductases - isolation & purification
Alcohol Oxidoreductases - metabolism
Alcohols - metabolism
Amino Sugars - metabolism
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Bacteriology
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
Cloning, Molecular
Dehydrogenase
Dehydrogenases
E coli
Enzymes
Escherichia coli
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
Gluconates - metabolism
Gluconobacter
Microbiology
Miscellaneous
Mission oriented research
Oxidation-Reduction
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Substrate Specificity
Xanthomonas campestris
Xanthomonas campestris - enzymology
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Summary:The chromosomal locus NP_636946 of Xanthomonas campestris DSM 3586 (ATCC 33913) which was earlier presumed to encode a quinoprotein glucose dehydrogenase has been cloned, expressed in Escherichia coli and the recombinant enzyme has been characterised. It was found to have no glucose dehydrogenase activity but to be active on many different polyols and diols, aliphatic alcohols, certain aldonic acids and amino-sugars. The product of D: -gluconic acid oxidation was 5-keto-D: -gluconic acid. The enzyme differs from polyol/gluconate dehydrogenases found in Gluconobacter by its single-chain architecture, different substrate specificity and much higher (20- to 30-fold) expression level in E.coli.
ISSN:0175-7598
1432-0614
DOI:10.1007/s00253-004-1775-3