Substrate Specificity of Alcohol Dehydrogenases

1993 ◽  
pp. 391-400 ◽  
Author(s):  
Bryce V. Plapp ◽  
David W. Green ◽  
Hong-Wei Sun ◽  
Doo-Hong Park ◽  
Keehyuk Kim
Keyword(s):  
Substrate Specificity ◽  
Alcohol Dehydrogenases

scholarly journals Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.

1987 ◽  
Vol 262 (8) ◽  
pp. 3754-3761
Author(s):  
A.J. Ganzhorn ◽  
D.W. Green ◽  
A.D. Hershey ◽  
R.M. Gould ◽  
B.V. Plapp
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Amino Acid Residue ◽  
Kinetic Characterization ◽  
Alcohol Dehydrogenases

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.

Modulating the catalytic activity and the substrate specificity of alcohol dehydrogenases using cyclic ethers

2015 ◽  
Vol 5 (8) ◽  
pp. 3922-3925 ◽  
Author(s):  
Norifumi Kawakami ◽  
Yosuke Hara ◽  
Kenji Miyamoto
Keyword(s):  
Catalytic Activity ◽  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Cyclic Ethers ◽  
Alcohol Dehydrogenases

The catalytic activity of Thermoanaerobacter brockii alcohol dehydrogenase (Tbadh) is increased by the addition of 1,3-dioxolane, although it is inhibited by the addition of tetrahydrofuran .

scholarly journals The Enzyme Activity and Substrate Specificity of Two Major Cinnamyl Alcohol Dehydrogenases in Sorghum (Sorghum bicolor), SbCAD2 and SbCAD4

2017 ◽  
Vol 174 (4) ◽  
pp. 2128-2145 ◽  
Author(s):  
Se-Young Jun ◽  
Alexander M. Walker ◽  
Hoon Kim ◽  
John Ralph ◽  
Wilfred Vermerris ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Substrate Specificity ◽  
Sorghum Bicolor ◽  
Cinnamyl Alcohol ◽  
Alcohol Dehydrogenases

Controlling Substrate Specificity and Stereospecificity of Alcohol Dehydrogenases

ACS Catalysis ◽  
2015 ◽  
Vol 5 (4) ◽  
pp. 2100-2114 ◽  
Author(s):  
Christopher M. Nealon ◽  
Musa M. Musa ◽  
Jay M. Patel ◽  
Robert S. Phillips
Keyword(s):  
Substrate Specificity ◽  
Alcohol Dehydrogenases
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