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1.14.99.1: prostaglandin-endoperoxide synthase

This is an abbreviated version!
For detailed information about prostaglandin-endoperoxide synthase, go to the full flat file.

Word Map on EC 1.14.99.1

Reaction

arachidonate
+
reduced acceptor
+ 2 O2 =
prostaglandin H2
+
acceptor
+
H2O

Synonyms

(PG)H synthase, COX, COX-1, COX-2, COX1, Cox2, cyclooxygenase, cyclooxygenase 1, cyclooxygenase 2, cyclooxygenase-1, cyclooxygenase-1b, cyclooxygenase-2, cycloxigenase-2, fatty acid cyclooxygenase, hPGHS-1, hPGHS-2, oPGHS-1, PG G/H synthase 2, PG H synthase, PG synthetase, PG-endoperoxide synthase 2, PG-endoperoxide synthetase, PGH-synthase, PGHS, PGHS isoform-1, PGHS-1, PGHS-2, PHS, PHS-1, PHS-2, prostagladin-H synthase, prostaglandin endoperoxide H synthase, prostaglandin endoperoxide H synthase 1, prostaglandin endoperoxide H synthase 2, prostaglandin endoperoxide H synthase-1, prostaglandin endoperoxide H2 synthase-2, prostaglandin endoperoxide synthase, prostaglandin endoperoxide synthase 2, prostaglandin endoperoxide synthase-1, prostaglandin endoperoxide synthase-2, prostaglandin endoperoxide synthetase, prostaglandin G/H synthase, prostaglandin G/H synthase-2, prostaglandin H synthase, prostaglandin H synthase-1, prostaglandin H synthase-2, prostaglandin H2 synthase, prostaglandin H2 synthase-1, prostaglandin synthase, prostaglandin synthase-2, prostaglandin synthetase, prostaglandin-endoperoxide synthase, prostaglandin-endoperoxide synthase 1, prostaglandin-endoperoxide synthase 2, prostaglandin-H-synthase, prostaglandin-H-synthase 1, prostaglandin-H-synthase 2, PTGS 2, PTGS-1, PTGS-2, PTGS1, PTGS2, putative cyclooxygenase-3, synthase, prostaglandin, tPGHS-1, tPGHS-2

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.99 Miscellaneous
                1.14.99.1 prostaglandin-endoperoxide synthase

General Information

General Information on EC 1.14.99.1 - prostaglandin-endoperoxide synthase

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the algal PGHS lacks structural elements identified in all known animal PGHSs, such as epidermal growth factor-like domain and helix B in the membrane binding domain. The key residues of animal PGHS, like catalytic Tyr385 and heme liganding His388 are conserved in the algal enzyme, but the amino acid residues shown to be important for substrate binding and coordination, and the target residues for nonsteroidal anti-inflammatory drugs, Arg120, Tyr355, and Ser530, are not found at the appropriate positions in the algal sequences. The preferred substrate for the algal PGHS is arachidonic acid with cyclooxygenase reaction rate remarkably higher than values reported for mammalian PGHS isoforms
malfunction
metabolism
physiological function
additional information