Purification, characterization, and cloning of a bifunctional molybdoenzyme with hydratase and alcohol dehydrogenase activity

A bifunctional hydratase/alcohol dehydrogenase was isolated from the cyclohexanol degrading bacterium Alicycliphilus denitrificans DSMZ 14773. The enzyme catalyzes the addition of water to α,β-unsaturated carbonyl compounds and the subsequent alcohol oxidation. The purified enzyme showed three subun...

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Detalles Bibliográficos
Autores principales: Jin, Jianfeng, Straathof, Adrie J. J., Pinkse, Martijn W. H., Hanefeld, Ulf
Formato: Texto
Lenguaje:English
Publicado: Springer-Verlag 2010
Materias:
Biotechnologically Relevant Enzymes and Proteins
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3044224/
https://www.ncbi.nlm.nih.gov/pubmed/21120472
http://dx.doi.org/10.1007/s00253-010-2996-2
Descripción
Sumario:A bifunctional hydratase/alcohol dehydrogenase was isolated from the cyclohexanol degrading bacterium Alicycliphilus denitrificans DSMZ 14773. The enzyme catalyzes the addition of water to α,β-unsaturated carbonyl compounds and the subsequent alcohol oxidation. The purified enzyme showed three subunits in SDS gel, and the gene sequence revealed that this enzyme belongs to the molybdopterin binding oxidoreductase family containing molybdopterins, FAD, and iron-sulfur clusters. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00253-010-2996-2) contains supplementary material, which is available to authorized users.

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