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Identification of an NADH-dependent 5-hydroxymethylfurfural-reducing alcohol dehydrogenase in Saccharomyces cerevisiae.

Laadan, Boaz LU ; Almeida, Joao LU ; Rådström, Peter LU ; Hahn-Hägerdal, Bärbel LU and Gorwa-Grauslund, Marie-Francoise LU (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)
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author
organization
publishing date
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
external identifiers
  • pmid:18302314
  • wos:000254806200003
  • scopus:41549139616
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
2008-03-25 15:00:17
date last changed
2017-11-19 03:44:26
@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},
  keyword      = {alcohol dehydrogenase,5-hydroxymethylfurfural,detoxification,lignocellulosic hydrolysates},
  language     = {eng},
  number       = {3},
  pages        = {191--198},
  publisher    = {John Wiley & Sons},
  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},
  volume       = {25},
  year         = {2008},
}