The pH Dependence of the Steady State Kinetic Parameters for Staphylococcal Nuclease-catalyzed Hydrolysis of Deoxythymidine-3′-phosphate-5′-p-nitrophenylphosphate in H2O and D2O
Year: 1973
Type: article
Abstract: Initial velocity studies over the pH range 7.5 to 10.5 have been utilized to derive kinetic constants for the hydrolysis of deoxythymidine-3'-phosphate-5'-p-nitrophenylphosphate catalyzed by staphylococcal nuclease. A pronounced decline in reaction rate at high substrate concentration has been attributed to multiple binding of the substrate to the enzyme. The pH dependence of the parameters κ2 and Km has been employed to derive kinetically apparent ionization constants for the processes of binding and reaction. This analysis also yielded the pH-independent kinetic constants κ2 in water and deuterium oxide with the ratio κ2h2o/κ2d2o = 0.95. The relationship of these data to the possible mechanism of catalysis has been considered.
Source: Journal of Biological Chemistry
Institution: National Institutes of Health
Language: English
Topic: Chemical Reaction Mechanisms
Subfield: Organic Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1544637166