Comparison of the properties of prostaglandin H synthase-1 and -2.
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.
Kulmacz
Richard J
RJ
Department of Internal Medicine, University of Texas Health Science Center at Houston, Houston, TX 77030, USA. richard.j.kulmacz@uth.tmc.edu
van der Donk
Wilfred A
WA
Tsai
Ah-Lim
AL
D000595:Amino Acid Sequence; D000818:Animals; D020134:Catalytic Domain; D051545:Cyclooxygenase 1; D051546:Cyclooxygenase 2; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000502:physiology*; D008565:Membrane Proteins; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D011451:Prostaglandin-Endoperoxide Synthases / Q000737:chemistry / Q000502:physiology*; D021382:Protein Sorting Signals / Q000502:physiology; D016415:Sequence Alignment; D013329:Structure-Activity Relationship
D007527:Isoenzymes; D008565:Membrane Proteins; D021382:Protein Sorting Signals; D051545:Cyclooxygenase 1; D051546:Cyclooxygenase 2; C496511:PTGS1 protein, human; C496540:PTGS2 protein, human; D011451:Prostaglandin-Endoperoxide Synthases