Partial Similarities Between Yeast and Liver Alcohol Dehydrogenases

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Partial similarities between yeast and liver alcohol dehydrogenases.

The primary structure of about half of the protein chain of yeast alcohol dehydrogenase has been determined and compared with the amino-acid sequences of other dehydrogenases. The enzyme is found to be distantly related to horse-liver alcohol dehydrogenase, although these two proteins have different quaternary structures and subunit sizes. Some regions show no significant similarities, but long...

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Inhibition by ethanol, acetaldehyde and trifluoroethanol of reactions catalysed by yeast and horse liver alcohol dehydrogenases.

1. Produced inhibition by ethanol of the acetaldehyde-NADH reaction, catalysed by the alcohol dehydrogenases from yeast and horse liver, was studied at 25 degrees C and pH 6-9. 2. The results with yeast alcohol dehydrogenase are generally consistent with the preferred-pathway mechanism proposed previously [Dickenson & Dickinson (1975) Biochem. J. 147, 303-311]. The observed hyperbolic inhibitio...

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Alcohol dehydrogenases and aldehyde dehydrogenases.

T h e structure, function and evolution of alcohol dehydrogenases and aldehyde dehydrogenases have been studied for several years. Recent progress o n these aspects has been considerable and allows extensive conclusions to be drawn about the relationships and properties of these enzymes. Further aspects have also become available for study, such as the regulation of enzyme expression and the an...

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Enzymatic and structural differences between usual and atypical human liver alcohol dehydrogenases.

It has been known that human cytosol alcohol dehydrogenase (alcoho1:NAD' oxidoreductase, EC 1.1.1.1), controlled by the ADHz locus, is polymorphic. Most Caucasians have enzyme Containing the usual PI subunit, while nearly 90% of Orientals have an enzyme containing the atypical / I 2 subunit. At physiological pH, the cytosol enzyme activity of atypical liver is much higher than that of typical l...

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Alcohol dehydrogenases.

9. Doonan, S., Martini, F., Angelaccio, S., Pascarella, S., Barra, D. & Bossa, F. ( 1986) J. Moi. Evol. 23, 328-335 McAllister-Henn, L. ( 1988) Trends Biocherrr. .ki . 13, 1781 8 1 Doyle, J. M. (1988) Ph.D. Thesis, National University of Ireland Martini, F., Angelaccio, S., Barra, D., Pascarella, S., Maras, B., Doonan. S. & Bossa, F. (1985) Hiochirn. Hiophys. Actcr 832, 46-5 I Lipman. D. J . & ...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 1973

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.70.8.2295