Substrate as a source of thermodynamic nonideality in enzyme kinetic studies: Invertase-catalyzed hydrolysis of sucrose

1988 ◽  
Vol 260 (2) ◽  
pp. 532-539 ◽  
Author(s):  
Keith E. Shearwin ◽  
Donald J. Winzor
Keyword(s):  
Kinetic Studies ◽  
Enzyme Kinetic ◽  
Hydrolysis Of ◽  
Thermodynamic Nonideality

Micellar catalysis of organic reactions. VIII. Kinetic studies of the hydrolysis of 2-acetyloxybenzoic acid (aspirin) in the presence of micelles

1982 ◽  
Vol 35 (7) ◽  
pp. 1357 ◽  
Author(s):  
TJ Broxton
Keyword(s):  
Aqueous Solution ◽  
Cetyltrimethylammonium Bromide ◽  
Cetylpyridinium Chloride ◽  
Kinetic Studies ◽  
Base Catalysis ◽  
Plateau Region ◽  
General Base ◽  
Mechanism Of Hydrolysis ◽  
Ph Range ◽  
Hydrolysis Of

The hydrolysis of 2-acetyloxybenzoic acid in the pH range 6-12 has been studied in the presence of micelles of cetyltrimethylammonium bromide (ctab) and cetylpyridinium chloride (cpc). In the plateau region (pH 6-8) the hydrolysis is inhibited by the presence of micelles, while in the region where the normal BAC2 hydrolysis (pH > 9) occurs the reaction is catalysed by micelles of ctab and cpc. The mechanism of hydrolysis in the plateau region is shown to involve general base catalysis by the adjacent ionized carboxy group both in the presence and absence of micelles. This reaction is inhibited in the presence of micelles because the substrate molecules are solubilized into the micelle and water is less available in this environment than in normal aqueous solution.

scholarly journals Stability of Indomethacin in Aqueous Solution. (1): Kinetic Studies and Effect of Solvents on the Hydrolysis of Indomethacin.

1992 ◽  
Vol 18 (1) ◽  
pp. 43-51 ◽  
Author(s):  
KAORU CHIBA ◽  
MASANAO TAKAHASHI ◽  
NOBUMASA HAYASE ◽  
SHIGETAKA AKUTSU ◽  
SHUNICHI INAGAKI
Keyword(s):  
Aqueous Solution ◽  
Kinetic Studies ◽  
Effect Of Solvents ◽  
Hydrolysis Of

scholarly journals Studies on the mechanism of sheep liver cytosolic aldehyde dehydrogenase

1985 ◽  
Vol 225 (1) ◽  
pp. 159-165 ◽  
Author(s):  
F M Dickinson
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Kinetic Studies ◽  
Dissociation Reaction ◽  
Quenching Effect ◽  
Sheep Liver ◽  
Association Reaction ◽  
Hydrolysis Of

The dissociation of the aldehyde dehydrogenase X NADH complex was studied by displacement with NAD+. The association reaction of enzyme and NADH was also studied. These processes are biphasic, as shown by McGibbon, Buckley & Blackwell [(1977) Biochem. J. 165, 455-462], but the details of the dissociation reaction are significantly different from those given by those authors. Spectral and kinetic experiments provide evidence for the formation of abortive complexes of the type enzyme X NADH X aldehyde. Kinetic studies at different wavelengths with transcinnamaldehyde as substrate provide evidence for the formation of an enzyme X NADH X cinnamoyl complex. Hydrolysis of the thioester relieves a severe quenching effect on the fluorescence of enzyme-bound NADH.

Cellular Regulation of the Metabolism of Androgens in Rat Oral Mucosa. III. Activation of Δ4-3-ketosteroid-5α-A Ring Reductase Enzyme System by 5,5-Diphenylhydantoin

1979 ◽  
Vol 58 (2) ◽  
pp. 642-645 ◽  
Author(s):  
Jozef Vittek ◽  
Gary G. Gordon ◽  
Sydney C. Rappaport ◽  
A. Louis Southren
Keyword(s):  
Oral Mucosa ◽  
Enzyme System ◽  
Kinetic Studies ◽  
In Vitro Assay ◽  
Enzyme Kinetic ◽  
Cellular Regulation ◽  
Vitro Assay ◽  
Allosteric Mechanism

Systemic pretreatment of rats with diphenylhydantoin (DPH) or its addition into an in vitro assay increases 5α-reduction of testosterone by the oral mucosa. Enzyme kinetic studies showed that DPH binds to the enzyme and probably activates it by an allosteric mechanism.

scholarly journals C-C Bond Fission in Carboxamides. Kinetic Studies on Alkaline Hydrolysis of Substituted α-Nitroisobutyranilides

1972 ◽  
Vol 45 (1) ◽  
pp. 203-208 ◽  
Author(s):  
Hiroteru Sayo ◽  
Hidenobu Ohomori ◽  
Tsuneji Umeda ◽  
Masaichiro Masui
Keyword(s):  
Alkaline Hydrolysis ◽  
Kinetic Studies ◽  
Hydrolysis Of
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