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Class III alcohol dehydrogenase from Saccharomyces cerevisiae : Structural and enzymatic features differ toward the human/mammalian forms in a manner consistent with functional needs in formaldehyde detoxication
Author(s) -
Rosario Fernández M.,
Biosca Josep A.,
Norin Annika,
Jörnvall Hans,
Parés Xavier
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00788-b
Subject(s) - alcohol dehydrogenase , detoxication , formaldehyde dehydrogenase , saccharomyces cerevisiae , enzyme , biochemistry , formaldehyde , alcohol , biology , chemistry , yeast , nad+ kinase
Alcohol dehydrogenase class III (glutathione‐dependent formaldehyde dehydrogenase) from Saccharomyces cerevisiae was purified and analyzed structurally and enzymatically. The corresponding gene was also analyzed after cloning from a yeast genome library by screening with a probe prepared through PCR amplification. As with class III alcohol dehydrogenase from other sources, the yeast protein was obtained in two active forms, deduced to reflect different adducts/modifications. Protein analysis established N‐terminal and C‐terminal positions, showing different and specific patterns in protein start positions between the human/mammalian, yeast, and prokaryotic forms. K m values with formaldehyde differ consistently, being about 10‐fold higher in the yeast than the human/mammalian enzymes, but compensated for by similar changes in κ cat values. This is compatible with the different functional needs, emphasizing low formaldehyde concentration in the animal cells but efficient formaldehyde elimination in the microorganisms. This supports a general role of the enzyme in formaldehyde detoxication rather than in long‐chain alcohol turnover.