Abstract

Aerobic yeast mitochondria contain a unique isozyme of acetaldehyde dehydrogenase that accounts for the ability of yeast mitochondria to respire with acetaldehyde as a substrate. Mitochondrial acetaldehyde dehydrogenase has a high affinity for acetaldehyde, is active with NAD+ and NADP+, is stimulated by K+, and appears to be the same acetaldehyde dehydrogenase previously isolated from yeast autolysates by Black ((1951) Arch. Biochem. Biophys. 34, 86–97) and Jakoby and coworkers (Steinman, C. R. and Jakoby, W. B. (1967) J. Biol. Chem. 242, 5019–5023; Steinman, C. R. and Jakoby, W. B. (1968) J. Biol. Chem. 243, 730–734; Clark, J. F. and Jakoby, W. B. (1970) J. Biol. Chem. 245, 6065–6071; Clark, J. F. and Jakoby, W. B. (1970) J. Biol. Chem. 245, 6072–6077; Bradbury, S. L. and Jakoby, W. B. (1971) J. Biol. Chem. 246, 1834–1840; Bradbury, S. L. and Jakoby, W. B. (1972) Proc. Natl. Acad. Sci. U.S. 69, 2373–2376). The enzyme is inhibited by Li+, Mg2+, and Disulfiram. Mitochondrial acetaldehyde dehydrogenase appears to play a role in the oxidative metabolism of ethanol, especially when yeast cells are utilizing ethanol as a source of carbon and energy for growth. The enzyme is more than 99% repressed during the growth of yeast on glucose.Yeast cells also contain a cytosol isozyme of acetaldehyde dehydrogenase that is active with NADP+, is stimulated by Mg2+, and is only partly repressed during growth on glucose. The cytosol isozyme resembles the acetaldehyde dehydrogenase previously prepared from yeast autolysates by Seegmiller ((1953) J. Biol. Chem. 201, 629–637).

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.