Alcohol dehydrogenase polymorphism inDrosophila: Enzyme kinetics of product inhibition

1988 ◽  
Vol 28 (1-2) ◽  
pp. 145-150 ◽  
Author(s):  
Pieter W. H. Heinstra ◽  
Willem Scharloo ◽  
George E. W. Thorig
Keyword(s):  
Alcohol Dehydrogenase ◽  
Enzyme Kinetics ◽  
Product Inhibition ◽  
Kinetics Of

scholarly journals Enzyme Kinetics of Native and Recombinant Secondary Alcohol Dehydrogenase originated from Micrococcus leuteus WIUJH20

2011 ◽  
Vol 25 (S1) ◽  
Author(s):  
Jenq‐Kuen Huang ◽  
Nick D Youngblut ◽  
Nicholas J Shoger ◽  
Vamshi Takkalpalli ◽  
Chi‐Tsai Lin ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Enzyme Kinetics ◽  
Secondary Alcohol ◽  
Secondary Alcohol Dehydrogenase ◽  
Kinetics Of

Kinetic Aspects of the Interaction of Blood Clotting Enzymes

1968 ◽  
Vol 19 (03/04) ◽  
pp. 364-367 ◽  
Author(s):  
H. C Hemker ◽  
P. W Hemker
Keyword(s):  
Enzyme Kinetics ◽  
Blood Clotting ◽  
Competitive Inhibition ◽  
Competitive Inhibitor ◽  
Kinetics Of

SummaryThe enzyme kinetics of competitive inhibition under conditions prevailing in clotting tests are developed and a method is given to measure relative amounts of a competitive inhibitor by means of the t — D plot.

Iodoacetate inactivation of rape alcohol dehydrogenase

1980 ◽  
Vol 45 (5) ◽  
pp. 1601-1607 ◽  
Author(s):  
Marie Stiborová ◽  
Sylva Leblová
Keyword(s):  
Alcohol Dehydrogenase ◽  
Protein Molecule ◽  
Sulfhydryl Groups ◽  
Inactivation Rate ◽  
First Order ◽  
Ph Dependent ◽  
Kinetics Of

Iodoacetate inactivates rape alcohol dehydrogenase (ADH, EC 1.1.1.1). The inactivation rate follows the kinetics of the first order, is pH-dependent, and decreases below pH 7.5. Besides irreversible alkylation of the sulfhydryl groups of the enzyme iodoacetate also forms a reversible complex with rape ADH. The coenzyme (NAD) and its analogs (ATP, ADP, AMP) competitively protect the enzyme against alkylation; o-phenanthroline also protects the enzyme against alkylation yet noncompetitively with respect to iodoacetate. Imidazole and o-phenanthroline compete with one another for binding to the protein molecule of rape ADH. Whereas o-phenanthroline decreases the inactivation rate imidazole increases the rate of iodoacetate inactivation.

scholarly journals Thermodynamics and Molecular Kinetics of Liver Alcohol Dehydrogenase.

1963 ◽  
Vol 17 supl. ◽  
pp. 27-33 ◽  
Author(s):  
Keith Dalziel ◽  
Gad Yagil ◽  
Warren F. Diven ◽  
Mark Takahashi
Keyword(s):  
Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Kinetics Of
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