Compounds similar in structure to reactants, intermediates and products of the aldolase-catalysed reaction were synthesized and their affinities for the enzyme determined. The best situations were found with bdicarbonyl phosphorylated compounds which are a good mimics of the incoming groups in the b
Kinetic analysis of enzyme reactions with slow-binding inhibition
✍ Scribed by Carmelo Garrido-del Solo; Francisco Garcı́a-Cánovas; Bent H. Havsteen; Ramón Varón Castellanos
- Book ID
- 108431586
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 201 KB
- Volume
- 51
- Category
- Article
- ISSN
- 0303-2647
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A general procedure is described for determining the kinetic constants of the slow, tight-binding inhibition of enzyme-catalyzed reactions by analyzing the data of initial and steady-state rate. All unknown parameters can be determined from several simple, sequential calculations. This method is sim
A method is proposed to determine the kinetic constants of enzyme modification where the condition of [Y0] >> [E0] is not satisfied, which is applicable to both inhibition and activation. This is a simple and rigorous one by which the apparent rate constants can be conveniently calculated, provided