Comparison of the properties of prostaglandin H synthase-1 and -2 |
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Authors: | Kulmacz Richard J van der Donk Wilfred A Tsai Ah-Lim |
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Affiliation: | Department of Internal Medicine, University of Texas Health Science Center at Houston, Houston, TX 77030, USA. richard.j.kulmacz@uth.tmc.edu |
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Abstract: | Biosynthesis of prostanoid lipid signaling agents from arachidonic acid begins with prostaglandin H synthase (PGHS), a hemoprotein in the myeloperoxidase family. Vertebrates from humans to fish have two principal isoforms of PGHS, termed PGHS-1 and-2. These two isoforms are structurally quite similar, but they have very different pathophysiological roles and are regulated very differently at the level of catalysis. The focus of this review is on the structural and biochemical distinctions between PGHS-1 and-2, and how these differences relate to the functional divergence between the two isoforms. |
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