A mathematical model of reaction-diffusion problem with Michaelis-Menten kinetics in catalyst particles arbitrary shape is investigated. Analytical expressions the concentration substrates are derived as functions Thiele modulus, modified Sherwood number, and Michaelis constant. Taylor series approach Akbari-Ganji's method utilized to determine substrate effectiveness factor. The effects factor...

Nearly 100 years ago Michaelis and Menten published their now classic paper [Michaelis, L., and Menten, M. L. (1913) Die Kinetik der Invertinwirkung. Biochem. Z. 49, 333-369] in which they showed that the rate of an enzyme-catalyzed reaction is proportional to the concentration of the enzyme-substrate complex predicted by the Michaelis-Menten equation. Because the original text was written in G...

in present study, the kinetic parameters of purified trypsin from pyloric caeca of common kilka (c.cultriventris caspia) were measured using the amidolytic (bapna) and esterolytic (tame) substrates. the results of the kinetic comparison between bapna and tame substrates showed that kinetic parameters including maximum velocity (vmax), catalytic constant (kcat) and catalytic efficiency (kcat/km)...

The kinetics of alpha-chymotrypsin (alpha-CT) catalyzed hydrolysis of 4-nitrophenyl acetate has been studied in aqueous solution of alkyldimethylethanolammonium bromide (cetyl, dodecyl, decyl) surfactants at concentrations below and above their critical micelle concentration. From Michaelis-Mcnten kinetics, the catalytic rate constant kcat and the Michaelis constant KM have been determined. The...

For enzymatic progress curves conforming to the Michaelis–Menten mechanism (E + S ES → E + P) under the experimental conditions where the substrate concentration is at least several times smaller than the Michaelis constant, the minimal fitting model cast as a system of numerically integrated differential equations is the simple ‘hit-and-run’ mechanism, E + S → E + P. The best-fit value of sing...

We present a quantitative analysis of recent data on the kinetics of ATP hydrolysis, which has presented a puzzle regarding the load dependence of the Michaelis constant. Within the framework of coarse grained two-state ratchet models, our analysis not only explains the puzzling data, but provides a modified Michaelis law, which could be useful as a guide for future experiments.

We have proposed the neck linker swing model to investigate the mechanism of mechanochemical coupling of kinesin. The Michaelis-Menten-like curve for velocity vs ATP concentration at different loads has been obtained, which is in agreement with experiments. We have predicted that Michaelis constant doesn’t increase monotonically and an elastic instability will happen with increasing of applied ...