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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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
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author Jin, Jianfeng
Straathof, Adrie J. J.
Pinkse, Martijn W. H.
Hanefeld, Ulf
author_facet Jin, Jianfeng
Straathof, Adrie J. J.
Pinkse, Martijn W. H.
Hanefeld, Ulf
author_sort Jin, Jianfeng
collection PubMed
description 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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spelling pubmed-30442242011-04-04 Purification, characterization, and cloning of a bifunctional molybdoenzyme with hydratase and alcohol dehydrogenase activity Jin, Jianfeng Straathof, Adrie J. J. Pinkse, Martijn W. H. Hanefeld, Ulf Appl Microbiol Biotechnol Biotechnologically Relevant Enzymes and Proteins 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. Springer-Verlag 2010-12-01 2011 /pmc/articles/PMC3044224/ /pubmed/21120472 http://dx.doi.org/10.1007/s00253-010-2996-2 Text en © The Author(s) 2010 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Biotechnologically Relevant Enzymes and Proteins
Jin, Jianfeng
Straathof, Adrie J. J.
Pinkse, Martijn W. H.
Hanefeld, Ulf
Purification, characterization, and cloning of a bifunctional molybdoenzyme with hydratase and alcohol dehydrogenase activity
title Purification, characterization, and cloning of a bifunctional molybdoenzyme with hydratase and alcohol dehydrogenase activity
title_full Purification, characterization, and cloning of a bifunctional molybdoenzyme with hydratase and alcohol dehydrogenase activity
title_fullStr Purification, characterization, and cloning of a bifunctional molybdoenzyme with hydratase and alcohol dehydrogenase activity
title_full_unstemmed Purification, characterization, and cloning of a bifunctional molybdoenzyme with hydratase and alcohol dehydrogenase activity
title_short Purification, characterization, and cloning of a bifunctional molybdoenzyme with hydratase and alcohol dehydrogenase activity
title_sort purification, characterization, and cloning of a bifunctional molybdoenzyme with hydratase and alcohol dehydrogenase activity
topic Biotechnologically Relevant Enzymes and Proteins
url 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
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