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

Yeast ◽  
1988 ◽  
Vol 4 (2) ◽  
pp. 143-148 ◽  
Author(s):  
Cornelis Verduyn ◽  
Guido J. Breedveld ◽  
W. Alexander Scheffers ◽  
Johnnes P. Van Dijken
Keyword(s):  
Alcohol Dehydrogenase ◽  
Substrate Specificity

Investigation of Structural Determinants for the Substrate Specificity in the Zinc-Dependent Alcohol Dehydrogenase CPCR2 fromCandida parapsilosis

ChemBioChem ◽  
2015 ◽  
Vol 16 (10) ◽  
pp. 1512-1519 ◽  
Author(s):  
Christoph Loderer ◽  
Gaurao V. Dhoke ◽  
Mehdi D. Davari ◽  
Wolfgang Kroutil ◽  
Ulrich Schwaneberg ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Structural Determinants

Structural insights into substrate specificity and solvent tolerance in alcohol dehydrogenase ADH-‘A’ from Rhodococcus ruber DSM 44541

2010 ◽  
Vol 46 (34) ◽  
pp. 6314 ◽  
Author(s):  
Martin Karabec ◽  
Andrzej Łyskowski ◽  
Katharina C. Tauber ◽  
Georg Steinkellner ◽  
Wolfgang Kroutil ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Solvent Tolerance ◽  
Rhodococcus Ruber ◽  
Structural Insights

Role of Tryptophan 95 in substrate specificity and structural stability of Sulfolobus solfataricus alcohol dehydrogenase

Extremophiles ◽  
2009 ◽  
Vol 13 (5) ◽  
pp. 751-761 ◽  
Author(s):  
Angela Pennacchio ◽  
Luciana Esposito ◽  
Adriana Zagari ◽  
Mosè Rossi ◽  
Carlo A. Raia
Keyword(s):  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Structural Stability ◽  
Sulfolobus Solfataricus

scholarly journals An Electrophoretically Cryptic Alcohol Dehydrogenase Variant in Drosophila Melanogaster. 11. Post-Electrophoresis Heat-Treatment Screening of Natural Populations

1980 ◽  
Vol 33 (5) ◽  
pp. 575 ◽  
Author(s):  
AV Wilks ◽  
JB Gibson ◽  
JG Oakeshott ◽  
GK Chambers
Keyword(s):  
Heat Treatment ◽  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Electrophoretic Mobility ◽  
Genetic Variants ◽  
Partial Correlation ◽  
Natural Populations ◽  
Maximum Temperature ◽  
Common Genetic Variants ◽  
Temperature Variable

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.

scholarly journals Structure and function of yeast alcohol dehydrogenase

2000 ◽  
Vol 65 (4) ◽  
pp. 207-227 ◽  
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 ◽  
Font Color

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 <br><br><font color="red"><b> This article has been corrected. Link to the correction <u><a href="http://dx.doi.org/10.2298/JSC0008609E">10.2298/JSC0008609E</a><u></b></font>

Regulation of NAD-specific alcohol dehydrogenases in Neurospora crassa

1969 ◽  
Vol 15 (3) ◽  
pp. 265-271 ◽  
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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