Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase

Enzymes of the non-conventional yeast Yarrowia lipolytica seem to be tailor-made for the conversion of lipophilic substrates. Herein, we cloned and overexpressed the Zn-dependent alcohol dehydrogenase ADH2 from Yarrowia lipolytica in Escherichia coli. The purified enzyme was characterized in vitro....

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Autores principales: Napora-Wijata, Kamila, Strohmeier, Gernot A., Sonavane, Manoj N., Avi, Manuela, Robins, Karen, Winkler, Margit
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
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Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4030946/
https://www.ncbi.nlm.nih.gov/pubmed/24970175
http://dx.doi.org/10.3390/biom3030449
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author Napora-Wijata, Kamila
Strohmeier, Gernot A.
Sonavane, Manoj N.
Avi, Manuela
Robins, Karen
Winkler, Margit
author_facet Napora-Wijata, Kamila
Strohmeier, Gernot A.
Sonavane, Manoj N.
Avi, Manuela
Robins, Karen
Winkler, Margit
author_sort Napora-Wijata, Kamila
collection PubMed
description Enzymes of the non-conventional yeast Yarrowia lipolytica seem to be tailor-made for the conversion of lipophilic substrates. Herein, we cloned and overexpressed the Zn-dependent alcohol dehydrogenase ADH2 from Yarrowia lipolytica in Escherichia coli. The purified enzyme was characterized in vitro. The substrate scope for YlADH2 mediated oxidation and reduction was investigated spectrophotometrically and the enzyme showed a broader substrate range than its homolog from Saccharomyces cerevisiae. A preference for secondary compared to primary alcohols in oxidation direction was observed for YlADH2. 2-Octanone was investigated in reduction mode in detail. Remarkably, YlADH2 displays perfect (S)-selectivity and together with a highly (R)-selective short chain dehydrogenase/ reductase from Yarrowia lipolytica it is possible to access both enantiomers of 2-octanol in >99% ee with Yarrowia lipolytica oxidoreductases.
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spelling pubmed-40309462014-06-24 Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase Napora-Wijata, Kamila Strohmeier, Gernot A. Sonavane, Manoj N. Avi, Manuela Robins, Karen Winkler, Margit Biomolecules Article Enzymes of the non-conventional yeast Yarrowia lipolytica seem to be tailor-made for the conversion of lipophilic substrates. Herein, we cloned and overexpressed the Zn-dependent alcohol dehydrogenase ADH2 from Yarrowia lipolytica in Escherichia coli. The purified enzyme was characterized in vitro. The substrate scope for YlADH2 mediated oxidation and reduction was investigated spectrophotometrically and the enzyme showed a broader substrate range than its homolog from Saccharomyces cerevisiae. A preference for secondary compared to primary alcohols in oxidation direction was observed for YlADH2. 2-Octanone was investigated in reduction mode in detail. Remarkably, YlADH2 displays perfect (S)-selectivity and together with a highly (R)-selective short chain dehydrogenase/ reductase from Yarrowia lipolytica it is possible to access both enantiomers of 2-octanol in >99% ee with Yarrowia lipolytica oxidoreductases. MDPI 2013-08-12 /pmc/articles/PMC4030946/ /pubmed/24970175 http://dx.doi.org/10.3390/biom3030449 Text en © 2013 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Napora-Wijata, Kamila
Strohmeier, Gernot A.
Sonavane, Manoj N.
Avi, Manuela
Robins, Karen
Winkler, Margit
Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase
title Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase
title_full Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase
title_fullStr Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase
title_full_unstemmed Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase
title_short Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase
title_sort enantiocomplementary yarrowia lipolytica oxidoreductases: alcohol dehydrogenase 2 and short chain dehydrogenase/reductase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4030946/
https://www.ncbi.nlm.nih.gov/pubmed/24970175
http://dx.doi.org/10.3390/biom3030449
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