A Michaelis-Menten-style model for the autocatalytic enzyme prostaglandin H synthase |
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| Authors: | Email author" target="_blank">Joseph?H?TienEmail author William?D?Hazelton Rachel?Sparks Cornelia?M?Ulrich |
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| Institution: | (1) Center for Applied Mathematics, Cornell University, 657 Frank H.T. Rhodes Hall, Ithaca, NY 14853, USA;(2) Fred Hutchinson Cancer Research Center, Public Health Sciences Division, P.O. Box 19024, M2-B500, Seattle, WA 98109-1024, USA;(3) Fred Hutchinson Cancer Research Center, Cancer Prevention, P.O. Box 19024, M4-B402, Seattle, WA 98109-1024, USA;(4) Present address: Division of Respiratory Disease Studies / Field Studies Branch, National Institute for Occupational Safety and Health, 1095 Willowdale Road, MS 2800, Morgantown, WV 26505, USA;(5) Department of Epidemiology, University of Washington, Seattle, WA 98195, USA |
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| 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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