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Literature summary for 1.14.99.1 extracted from

  • Roth, G.J.; Siok, C.J.; Ozols, J.
    Structural characteristics of prostaglandin synthetase from sheep vesicular gland (1980), J. Biol. Chem., 255, 1301-1304.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Acetylsalicylic acid inhibition of oxygenase activity by acetylating a serine residue of the enzyme Ovis aries

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Ovis aries
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
72000
-
x * 72000, SDS-PAGE, oxygenase and peroxidase activity are present in a single polypeptide chain, in nonionic detergent the enzyme is a dimer of 2 identical subunits Ovis aries

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Ovis aries first step in prostaglandin synthesis ?
-
?

Organism

Organism UniProt Comment Textmining
Ovis aries
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Ovis aries

Source Tissue

Source Tissue Comment Organism Textmining
seminal vesicle
-
Ovis aries
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
43
-
-
Ovis aries

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information first step in prostaglandin synthesis Ovis aries ?
-
?

Subunits

Subunits Comment Organism
? x * 72000, SDS-PAGE, oxygenase and peroxidase activity are present in a single polypeptide chain, in nonionic detergent the enzyme is a dimer of 2 identical subunits Ovis aries