The Stereospecificity of Hydrogen Transfer to NAD(P)+Catalyzed by Lactol Dehydrogenases

The stereochemistry of hydrogen transfer to NAD(P)+has been determined for five lactol dehydrogenases. It was found that D-glucose dehydrogenases fromBacillus megateriumandCryptococcus uniguttulatusand L-rhamnose dehydrogenase fromAureobasidium pullulansarepro-S(B) specific, while D-glucose dehydrog...

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Published inBiochemical and biophysical research communications Vol. 233; no. 3; pp. 681 - 686
Main Authors Mostad, Sara B., Helming, Heather L., Groom, Corwin, Glasfeld, Arthur
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 28.04.1997
Subjects
Animals
Bacillus megaterium - enzymology
Carbohydrate Dehydrogenases - metabolism
Cryptococcus - enzymology
Hydrogen - metabolism
Liver - enzymology
Magnetic Resonance Spectroscopy
Mitosporic Fungi - enzymology
NAD - chemistry
NAD - metabolism
NADP - chemistry
NADP - metabolism
Stereoisomerism
Substrate Specificity
Swine
Thermoplasma - enzymology
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Summary:The stereochemistry of hydrogen transfer to NAD(P)+has been determined for five lactol dehydrogenases. It was found that D-glucose dehydrogenases fromBacillus megateriumandCryptococcus uniguttulatusand L-rhamnose dehydrogenase fromAureobasidium pullulansarepro-S(B) specific, while D-glucose dehydrogenase fromThermoplasma acidophilumand D-xylose dehydrogenase from porcine liver arepro-R(A) specific. The latter two enzymes are the first examples of A-specific dehydrogenases oxidizing aldoses at the anomeric carbon. These findings are discussed in terms of functional and historical models that seek to make predictive generalizations regarding dehydrogenase stereospecificity.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1997.6519