Substrate specificity of alcohol dehydrogenase from the yeastHansenyls polymorpha CBS 4732 andCandida utilis CBS 621

The two common genetic variants of alcohol dehydrogenase in D. melanogaster, ADH-F and ADH-S, differ in substrate specificity and electrophoretic mobility. A third inherited variant, ADH-FCh.D., has a substrate specificity like ADH-S, an electrophoretic mobility like ADH-F, but much greater thermostability than either of the others. ADH-FCh.D. can be identified after post-electrophoresis heat treatment (15 s at 43�C) on cellulose acetate sheets. The AdhFCh?D ? allele has been found in 19 of 34 natural populations in Australasia but its frequency in these populations does not exceed 0�06. The partial correlation between AdhFCh ?D ? frequency and a maximum temperature variable is significant and positive among the Australasian populations although different climatic associations are found for a thermostable form of ADH-F in North America.

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Structure and function of yeast alcohol dehydrogenase

Journal of the Serbian Chemical Society ◽

10.2298/jsc0004207t ◽

2000 ◽

Vol 65 (4) ◽

pp. 207-227 ◽

Cited By ~ 9

Author(s):

Svetlana Trivic ◽

Vladimir Leskovac

Keyword(s):

Alcohol Dehydrogenase ◽

Substrate Specificity ◽

Primary Structure ◽

Active Site ◽

Hydride Transfer ◽

Kinetic Mechanism ◽

Structure And Function ◽

Chemical Mechanism ◽

And Function ◽

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1. Introduction 2. Isoenzymes of YADH 3. Substrate specificity 4. Kinetic mechanism 5. Primary structure 6. The active site 7. Mutations in the yeast enzyme 8. Chemical mechanism 9. Binding of coenzymes 10. Hydride transfer This article has been corrected. Link to the correction <a href="http://dx.doi.org/10.2298/JSC0008609E">10.2298/JSC0008609E</a>

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HETEROGENEITY, POLYMORPHISM, AND SUBSTRATE SPECIFICITY OF ALCOHOL DEHYDROGENASE FROM HORSE LIVER

Isozymes ◽

10.1016/b978-0-12-472701-4.50049-8 ◽

1975 ◽

pp. 707-724 ◽

Cited By ~ 2

Author(s):

REGINA PIETRUSZKO

Keyword(s):

Alcohol Dehydrogenase ◽

Substrate Specificity ◽

Horse Liver

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Regulation of NAD-specific alcohol dehydrogenases in Neurospora crassa

Canadian Journal of Microbiology ◽

10.1139/m69-049 ◽

1969 ◽

Vol 15 (3) ◽

pp. 265-271 ◽

Cited By ~ 6

Author(s):

M. W. Zink

Keyword(s):

Carbon Source ◽

Alcohol Dehydrogenase ◽

Substrate Specificity ◽

Neurospora Crassa ◽

Sole Source ◽

Protein Band ◽

Alcohol Dehydrogenases

Neurospora crassa is capable of synthesizing two different alcohol dehydrogenases. The synthesis of each depends upon the carbon source on which the mycelium is grown. The fermentative alcohol dehydrogenase, consisting of one electrophoretic protein band, is produced when the mycelium is grown on sucrose. The oxidative alcohol dehydrogenase, consisting of at least two isozymes, is synthesized when Neurospora crassa is grown on ethanol as a sole source of carbon. This latter enzyme is repressed by sugars such as glucose or sucrose. The two enzymes have been differentiated (1) electrophoretically, (2) by their substrate specificity, (3) by the ratio of the forward and reverse reactions, and (4) by their thermostability. Extracts from acetate-grown cells indicate a mixture of the two enzymes.

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