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Masayuki KUSANO, Yasuyoshi SAKAI, Nobuo KATO, Hiroyuki YOSHIMOTO, Hidetaka SONE, Yukio TAMAI, Hemiacetal Dehydrogenation Activity of Alcohol Dehydrogenases in Saccharomyces cerevisiae, Bioscience, Biotechnology, and Biochemistry, Volume 62, Issue 10, 1 January 1998, Pages 1956–1961, https://doi.org/10.1271/bbb.62.1956
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Abstract
Some methylotrophic yeasts produce methyl formate from methanol and formaldehyde via hemiacetal formation. We investigated Saccharomyces cerevisiae to find whether this yeast has a carboxylate ester producing pathway that proceeds via hemiacetal dehydrogenation. We confirmed that the purified alcohol dehydrogenase (Adh) protein from S. cerevisiae can catalyze the production of esters. High specific activities were observed toward the hemiacetals corresponding to the primary alcohols when ether groups were substituted for methylene groups, resulting in the formation of formate esters. Both ADH and methyl formate synthesizing activities were sharply reduced in the Δadh1 Δadh2 mutant. The ADH1 and ADH2 genes encode the major Adh proteins in S. cerevisiae. Thus, it was concluded that the S. cerevisiae Adh protein catalyzes activities for the production of certain carboxylate esters.
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