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Literature summary extracted from

  • Haeggström, J.Z.; Wetterholm, A.; Shapiro, R.; Vallee, B.L.; Samuelsson, B.
    Leukotriene A4 hydrolase: a zinc metalloenzyme (1990), Biochem. Biophys. Res. Commun., 172, 965-970.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.3.2.6 medicine the enzyme catalyses the hydrolysis of leukotriene A4 into the proinflammatory substance leukotriene B4 Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.3.2.6 1,10-phenanthroline
-
 Homo sapiens
3.3.2.6 8-Hydroxy-quinoline-5-sulfonic acid
-
 Homo sapiens
3.3.2.6 additional information not: EDTA, dipicolinic acid Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.3.2.6 Zinc zinc content: 1 mol of zinc per mol of enzyme Homo sapiens
3.3.2.6 Zinc zinc protein Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.3.2.6 leukotriene A4 + H2O Homo sapiens biosynthesis of leukotriene B4 leukotriene B4
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.3.2.6 Homo sapiens
-
-
-

Storage Stability

EC Number Storage Stability Organism
3.3.2.6 4°C, 25 mM HEPES, pH 8.0 the apoenzyme is stable for more than 5 weeks Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.3.2.6 leukotriene A4 + H2O
-
 Homo sapiens leukotriene B4
-
 ?
3.3.2.6 leukotriene A4 + H2O biosynthesis of leukotriene B4 Homo sapiens leukotriene B4
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.3.2.6 0.0003
-
 1,10-phenanthroline pH 8.0, 22°C Homo sapiens