Aldehyde dismutase activity of yeast alcohol dehydrogenase

@article{Trivi2004AldehydeDA,
  title={Aldehyde dismutase activity of yeast alcohol dehydrogenase},
  author={Svetlana Trivi{\'c} and Vladimir Leskova and Gary W. Winston},
  journal={Biotechnology Letters},
  year={2004},
  volume={21},
  pages={231-234}
}
Yeast alcohol dehydrogenase (EC 1.1.1.1) is able to catalyze the oxidation of acetaldehyde by NAD+ with a concomitant formation of ethanol, at pH 8.8 and pH 7.1; the stoichiometry of aldehyde oxidation vs. ethanol formation is 2:1. This enzymatic reaction obeys the Michaelis-Menten kinetics and was characterized by a high KM for acetaldehyde (68 mM) and a low kcat (2.3 s−1), at pH 8.8, 22 °C. There is no visible burst of NADH during the reaction, from pH 7.1–10.1. Therefore, we have concluded… CONTINUE READING