Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.3.99.5 extracted from

  • Yeh, H.C.; Tsai, A.L.; Wang, L.H.
    Reaction mechanisms of 15-hydroperoxyeicosatetraenoic acid catalyzed by human prostacyclin and thromboxane synthases (2007), Arch. Biochem. Biophys., 461, 159-168.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.3.99.5

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.071
-
 15-hydroperoxyeicosatetraenoic acid pH 7.5, 23°C, heterolytic cleavage Homo sapiens
0.087
-
 15-hydroperoxyeicosatetraenoic acid pH 7.5, 23°C, homolytic cleavage Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 recombinant enzyme
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
15-hydroperoxyeicosatetraenoic acid
-
 Homo sapiens 13-hydroxy-14,15-epoxy-5,8,11-eicosatrienoic acid + 15-ketoeicosatetraenoic acid + 13-hydroxy-14,15-epoxy-5,8,11-eicosatrienoic acid + 15-ketoeicosatetraenoic acid 13-hydroxy-14,15-epoxy-5,8,11-eicosatrienoic acid and 15-ketoeicosatetraenoic acid result from homolytic cleavage of the O-O bond, whereas 13-hydroxy-14,15-epoxy-5,8,11-eicosatrienoic acid + 15-ketoeicosatetraenoic acid results from heterolytic cleavage. About 60% of substrate is cleaved homolytically, and maximal velocity of homolytic cleavage is about 1.4fold faster than heterolytic cleavage ?