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Updated: Aug 18, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
A Michaelis-Menten-style model for the autocatalytic enzyme prostaglandin H synthase
Joseph H Tien1, William D Hazelton, Rachel Sparks
1Center for Applied Mathematics, Cornell University, 657 Frank H.T. Rhodes Hall, Ithaca, NY 14853, USA. joetien@cam.cornell.edu
Abstract:
Prostaglandin H synthase (PGHS) is an autocatalytic enzyme which plays a key role in the arachidonic acid metabolic pathway. PGHS mediates the formation of prostaglandin H2, the precursor for a number of prostaglandins which are important in a wide variety of biological processes, including inflammation, blood clotting, renal function, and tumorigenesis. Here we present a Michaelis-Menten-style model for PGHS. A stability analysis determines when the reaction becomes self-sustaining, and can help explain the regulation of PGHS activity in vivo. We also consider a quasi-steady-state approximation (QSSA) for the model, and present conditions under which the QSSA is expected to be a good approximation. Applying the QSSA for this model can be useful in computationally intensive modeling endeavors involving PGHS.
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