Open AccessCharacterization of a Saccharomyces cerevisiae NADP(H)‐dependent alcohol dehydrogenase (ADHVII), a member of the cinnamyl alcohol dehydrogenase family
Author(s) -
Larroy Carol,
Parés Xavier,
Biosca Josep A
Publication year - 2002
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1033.2002.03296.x
Subject(s) - alcohol dehydrogenase , saccharomyces cerevisiae , biochemistry , yeast , enzyme , dehydrogenase , cinnamyl alcohol dehydrogenase , chemistry , alcohol oxidoreductase , biology , nad+ kinase , biosynthesis
A new NADP(H)‐dependent alcohol dehydrogenase (the YCR105W gene product, ADHVII) has been identified in Saccharomyces cerevisiae . The enzyme has been purified to homogeneity and found to be a homodimer of 40 kDa subunits and a pI of 6.2–6.4. ADHVII shows a broad substrate specificity similar to the recently characterized ADHVI (64% identity), although they show some differences in kinetic properties. ADHVI and ADHVII are the only members of the cinnamyl alcohol dehydrogenase family in yeast. Simultaneous deletion of ADH6 and ADH7 was not lethal for the yeast. Both enzymes could participate in the synthesis of fusel alcohols, ligninolysis and NADP(H) homeostasis.