Chemical grafting of functional NAD in the active site of a dehydrogenase regeneration in situ

A functional NAD molecule was immobilized at the active site of Alcohol dehydrogenase within a proteic membrane. The presence and the functionality of the cofactor was checked by fluorescence analysis. The dehydrogenase NAD membrane does not require addition of soluble cofactor for its activity. The...

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Bibliographic Details
Published inFEBS letters Vol. 94; no. 2; pp. 335 - 338
Main Authors Marie-Dominique, Legoy, Jean-Michel, Le Moullec, Daniel, Thomas
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 15.10.1978
Subjects
Alcohol Oxidoreductases - metabolism
Binding Sites
Enzymes, Immobilized - metabolism
Methylphenazonium Methosulfate
NAD - metabolism
Oxidation-Reduction
Spectrometry, Fluorescence
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Summary:A functional NAD molecule was immobilized at the active site of Alcohol dehydrogenase within a proteic membrane. The presence and the functionality of the cofactor was checked by fluorescence analysis. The dehydrogenase NAD membrane does not require addition of soluble cofactor for its activity. The system represents a new worthwhile approach because both problems of retention and regeneration of cofactor are solved. The method can be used not only for industrial and analytical applications but also to try to get a better understanding of the kinetics and mechanisms of the catalytic action of dehydrogenase.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(78)80970-3