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Literature summary for 3.3.2.6 extracted from

  • Bito, H.; Ohishi, N.; Miki, I.; Minami, M.; Tanabe, T.; Shimizu, T.; Seyama, Y.
    Leukotriene A4 hydrolase from guinea pig lung: the presence of two catalytically active forms (1989), J. Biochem., 105, 261-264.
    View publication on PubMed

Application

Application Comment Organism
medicine the enzyme catalyses the hydrolysis of leukotriene A4 into the proinflammatory substance leukotriene B4 Cavia porcellus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.017
-
leukotriene A4 pH 7.8, 37°C Cavia porcellus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
gel filtration Cavia porcellus
70000
-
x * 70000, SDS-PAGE Cavia porcellus

Organism

Organism UniProt Comment Textmining
Cavia porcellus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Cavia porcellus

Source Tissue

Source Tissue Comment Organism Textmining
lung
-
Cavia porcellus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.53
-
-
Cavia porcellus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
leukotriene A4 + H2O
-
Cavia porcellus leukotriene B4
-
?

Subunits

Subunits Comment Organism
? x * 70000, SDS-PAGE Cavia porcellus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6 8.9
-
Cavia porcellus

pI Value

Organism Comment pI Value Maximum pI Value
Cavia porcellus chromatofocusing, isoelectric focusing, in absence of SH reducing reagents
-
5.4
Cavia porcellus chromatofocusing, isoelectric focusing, in presence of SH reducing reagents
-
5.7