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Literature summary extracted from

  • Li, Y.C.; Chiang, C.W.; Yeh, H.C.; Hsu, P.Y.; Whitby, F.G.; Wang, L.H.; Chan, N.L.
    Structures of prostacyclin synthase and its complexes with substrate-analog and inhibitor reveal a ligand-specific heme conformation change (2008), J. Biol. Chem., 283, 2917-2926.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.99.4 expression in Escherichia coli Danio rerio

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.99.4 recombinant protein without ligand, in complex with inhibitor minoxidil, or with substrate analogue U51605. Upon stereo-specific binding of substrate, conformational changes take place at the proximal side and in the heme itself. Mechanism is a radical-mediated isomerization with high product fidelity Danio rerio

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.3.99.4 minoxidil
-
 Danio rerio

Organism

EC Number Organism UniProt Comment Textmining
5.3.99.4 Danio rerio
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.99.4 recombinant enzyme Danio rerio

Reaction

EC Number Reaction Comment Organism Reaction ID
5.3.99.4 (5Z,13E,15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E,15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoate radical-mediated isomerizytion with high product fidelity Danio rerio
a