Mechanistic deductions from multiple kinetic and solvent deuterium isotope effects and pH studies of pyridoxal phosphate dependent carbon-carbon lyases: Escherichia coli tryptophan indole-lyase

Biochemistry ◽  
1988 ◽  
Vol 27 (19) ◽  
pp. 7339-7344 ◽  
Author(s):  
Dennis M. Kiick ◽  
Robert S. Phillips
Keyword(s):  
Escherichia Coli ◽  
Pyridoxal Phosphate ◽  
Isotope Effects ◽  
Deuterium Isotope Effects

Deuterium isotope effects on β-galactosidase formation by Escherichia coli

1967 ◽  
Vol 120 (2) ◽  
pp. 316-321 ◽  
Author(s):  
T.R. Henderson ◽  
Judy M. Dacus ◽  
H.L. Crespi ◽  
J.J. Katz
Keyword(s):  
Escherichia Coli ◽  
Isotope Effects ◽  
Deuterium Isotope Effects

Mechanism of hydration and isomerisation of 4-ethylidene-2,6-di-tert-butyl-2,5-cyclohexadien-1-one. Kinetics, acid-base catalysis and solvent deuterium isotope effects

1979 ◽  
Vol 44 (1) ◽  
pp. 110-122 ◽  
Author(s):  
Jiří Velek ◽  
Bohumír Koutek ◽  
Milan Souček
Keyword(s):  
Aqueous Medium ◽  
Rate Equation ◽  
Kinetic Data ◽  
Isotope Effects ◽  
Base Catalysis ◽  
Quinone Methide ◽  
Reaction Products ◽  
Acid Base ◽  
Deuterium Isotope Effects ◽  
Hydroxybenzyl Alcohol

Competitive hydration and isomerisation of the quinone methide I at 25 °C in an aqueous medium in the region of pH 2.4-13.0 was studied spectrophotometrically. The only reaction products in the studied range of pH are 4-hydroxybenzyl alcohol (II) and 4-hydroxystyrene (III). The form of the overall rate equation corresponds to a general acid-base catalysis. The mechanism of both reactions for three markedly separated pH regions is discussed on the basis of kinetic data and solvent deuterium effect.

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