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Inhibition of nicotinoprotein (NAD+-containing) alcohol dehydrogenase by trans-4- (N,N-dimethylamino) -cinnamaldehyde binding to the active site

Piersma, S.R.; Norin, A.; de Vries, S.; Jörnvall, H.; Duine, J.A.

Journal of Protein Chemistry 22(5): 457-461

2003


ISSN/ISBN: 0277-8033
PMID: 14690248
DOI: 10.1023/b:jopc.0000005461.53788.ee
Accession: 012216258

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Ethanol oxidation by nicotinoprotein alcohol dehydrogenase (np-ADH) from the bacterium Amycolatopsis methanolica is inhibited by trans-4-(N,N-dimethylamino)-cinnamaldehyde through direct binding to the catalytic zinc ion in a substrate-like geometry. This binding is accompanied by a characteristic red shift of the aldehyde absorbance from 398 nm to 467 nm.

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