Literature summary for 5.3.99.4 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Danio rerio

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Inhibitors	Comment	Organism	Structure
minoxidil	-	Danio rerio

Organism

Organism	UniProt	Comment	Textmining
Danio rerio	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme	Danio rerio

Reaction

Reaction	Comment	Organism	Reaction ID
(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

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Release 2023.1 (January 2023)