Identification of an NADH-dependent 5-hydroxymethylfurfural-reducing alcohol dehydrogenase in Saccharomyces cerevisiae.
(2008) In Yeast 25(3). p.191-198- Abstract
- We report on the identification and characterization of a mutated alcohol dehydrogenase 1 from the industrial Saccharomyces cerevisiae strain TMB3000 that mediates the NADH-dependent reduction of 5-hydroxymethylfurfural (HMF) to 2,5-bis-hydroxymethylfuran. The co-factor preference distinguished this alcohol dehydrogenase from the previously reported NADPH-dependent S. cerevisiae HMF alcohol dehydrogenase Adh6. The amino acid sequence revealed three novel mutations (S109P, L116S and Y294C) that were all predicted at the vicinity of the substrate binding site, which could explain the unusual substrate specificity. Increased biomass production and HMF conversion rate were achieved in a CEN.PK S. cerevisiae strain overexpressing the mutated... (More)
- We report on the identification and characterization of a mutated alcohol dehydrogenase 1 from the industrial Saccharomyces cerevisiae strain TMB3000 that mediates the NADH-dependent reduction of 5-hydroxymethylfurfural (HMF) to 2,5-bis-hydroxymethylfuran. The co-factor preference distinguished this alcohol dehydrogenase from the previously reported NADPH-dependent S. cerevisiae HMF alcohol dehydrogenase Adh6. The amino acid sequence revealed three novel mutations (S109P, L116S and Y294C) that were all predicted at the vicinity of the substrate binding site, which could explain the unusual substrate specificity. Increased biomass production and HMF conversion rate were achieved in a CEN.PK S. cerevisiae strain overexpressing the mutated ADH1 gene. Copyright (c) 2008 John Wiley & Sons, Ltd. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1041475
- author
- Laadan, Boaz LU ; Almeida, Joao LU ; Rådström, Peter LU ; Hahn-Hägerdal, Bärbel LU and Gorwa-Grauslund, Marie-Francoise LU
- organization
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- alcohol dehydrogenase, 5-hydroxymethylfurfural, detoxification, lignocellulosic hydrolysates
- in
- Yeast
- volume
- 25
- issue
- 3
- pages
- 191 - 198
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- pmid:18302314
- wos:000254806200003
- scopus:41549139616
- pmid:18302314
- ISSN
- 1097-0061
- DOI
- 10.1002/yea.1578
- language
- English
- LU publication?
- yes
- id
- d76d3bb0-ae94-4bbd-a24d-f4f92af333e2 (old id 1041475)
- date added to LUP
- 2016-04-01 13:14:27
- date last changed
- 2022-04-21 20:35:19
@article{d76d3bb0-ae94-4bbd-a24d-f4f92af333e2,
abstract = {{We report on the identification and characterization of a mutated alcohol dehydrogenase 1 from the industrial Saccharomyces cerevisiae strain TMB3000 that mediates the NADH-dependent reduction of 5-hydroxymethylfurfural (HMF) to 2,5-bis-hydroxymethylfuran. The co-factor preference distinguished this alcohol dehydrogenase from the previously reported NADPH-dependent S. cerevisiae HMF alcohol dehydrogenase Adh6. The amino acid sequence revealed three novel mutations (S109P, L116S and Y294C) that were all predicted at the vicinity of the substrate binding site, which could explain the unusual substrate specificity. Increased biomass production and HMF conversion rate were achieved in a CEN.PK S. cerevisiae strain overexpressing the mutated ADH1 gene. Copyright (c) 2008 John Wiley & Sons, Ltd.}},
author = {{Laadan, Boaz and Almeida, Joao and Rådström, Peter and Hahn-Hägerdal, Bärbel and Gorwa-Grauslund, Marie-Francoise}},
issn = {{1097-0061}},
keywords = {{alcohol dehydrogenase; 5-hydroxymethylfurfural; detoxification; lignocellulosic hydrolysates}},
language = {{eng}},
number = {{3}},
pages = {{191--198}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Yeast}},
title = {{Identification of an NADH-dependent 5-hydroxymethylfurfural-reducing alcohol dehydrogenase in Saccharomyces cerevisiae.}},
url = {{http://dx.doi.org/10.1002/yea.1578}},
doi = {{10.1002/yea.1578}},
volume = {{25}},
year = {{2008}},
}