Premium
Identification of an NADH‐dependent 5‐hydroxymethylfurfural‐reducing alcohol dehydrogenase in Saccharomyces cerevisiae
Author(s) -
Laadan Boaz,
Almeida João R. M.,
Rådström Peter,
HahnHägerdal Bärbel,
GorwaGrauslund Marie
Publication year - 2008
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.1578
Subject(s) - alcohol dehydrogenase , saccharomyces cerevisiae , biochemistry , biology , dehydrogenase , enzyme , nad+ kinase , substrate (aquarium) , strain (injury) , gene , ecology , anatomy
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 © 2008 John Wiley & Sons, Ltd.