ChemRxiv
These are preliminary reports that have not been peer-reviewed. They should not be regarded as conclusive, guide clinical practice/health-related behavior, or be reported in news media as established information. For more information, please see our FAQs.
sm_8-preprint.pdf (457.73 kB)
0/0

Theory of the reactant-stationary kinetics for a coupled enzyme assay

preprint
revised on 23.06.2018 and posted on 25.06.2018 by Justin Eilertsen, Wylie Stroberg, Santiago Schnell
A theoretical analysis is performed on the nonlinear ordinary differential equations that govern the dynamics of a coupled auxiliary enzyme catalyzed reaction. The assay consists of a non-observable reaction and an indicator (observable) reaction, where the product of the first reaction is the enzyme for the second. Both reactions are governed by the single substrate, single enzyme Michaelis-Menten reaction mechanism. Using singular perturbation methods, we derive asymptotic solutions that are valid under the quasi-steady-state and reactant-stationary assumptions. In particular, we obtain closed form solutions, analogous to the Schnell-Mendoza equation for Michaelis-Menten type reactions, that approximate the evolution of the observable reaction. Conditions for the validity of the asymptotic solutions are also rigorously derived showing that these asymptotic expressions are applicable under the reactant-stationary kinetics.

Funding

NIH/NIGMS K12 GM111725; University of Michigan Protein Folding Disease Initiative

History

Email Address of Submitting Author

schnells@umich.edu

Email Address(es) for Other Author(s)

jueilert@umich.edu; stroberg@umich.edu

Institution

University of Michigan Medical School, Ann Arbor, MI

Country

USA

ORCID For Submitting Author

0000-0002-9477-3914

Declaration of Conflict of Interest

No conflict of interest.

Licence

Exports