Michaelis-Menten(MM)enzyme kinetics is and has been widely used since early 20th century.However,the conventional enzyme kinetics is not accurate when the substrate is not in excess or when the steady-state approximation does not hold.The steady-state approximation worsens as the enzyme concentration exceeds its substrate concentration,which is the case in many biological processes.Here,to overcome this issue,we present a novel,quasi-exact solution of the enzyme kinetic equations,which provides the time profiles of the substrate,enzyme-substrate complex,and product concentrations.Our theory provides more accurate results than the previously reported theories for all parameter spaces investigated and yields a new relationship of the enzyme reaction time or the enzyme reaction rate to the substrate and enzyme concentrations.We demonstrate our results for the catalytic reaction of p-galactosidase.
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