US EPA

1182441 

Journal Article 

Hemiacetal dehydrogenation activity of alcohol dehydrogenases in Saccharomyces cerevisiae 

Kusano, M; Sakai, Y; Kato, N; Yoshimoto, H; Sone, H; Tamai, Y 

1998 

Yes 

Bioscience, Biotechnology, and Biochemistry
ISSN: 0916-8451
EISSN: 1347-6947 

62 

10 

1956-1961 

English 

9836432 

10.1271/bbb.62.1956 

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 delta adh1 delta adh2 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. 

alcohol dehydrogenase; Saccharomyces cerevisiae; carboxylate ester synthesis; hemiacetal dehydrogenation