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Novel substrates of yeast alcohol dehydrogenase‐4. Allyl alcohol and ethylene glycol
Author(s) -
Trivic Svetlana,
Leskovac Vladimir
Publication year - 1999
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549900201003
Subject(s) - ethylene glycol , alcohol dehydrogenase , acrolein , alcohol , allyl alcohol , chemistry , yeast , ethanol , nad+ kinase , ethylene , alcohol oxidoreductase , catalysis , organic chemistry , enzyme , biochemistry
In the present work, we have determined the steady‐state kinetic constants for yeast alcohol dehydrogenase‐catalyzed oxidation of allyl alcohol (H2C=CH.CH2OH) and ethylene glycol (HOCH2.CH2OH) with NAD+, at pH 8.0; also, a kinetic mechanism for the former reaction was determined at the same pH. In addition, it was found that acrolein is a potent inhibitor of yeast alcohol de‐hydrogenase.