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Literature summary for 3.3.2.6 extracted from

  • Thangapandian, S.; John, S.; Lazar, P.; Choi, S.; Lee, K.W.
    Structural origins for the loss of catalytic activities of bifunctional human LTA4H revealed through molecular dynamics simulations (2012), PLoS ONE, 7, e41063.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
E271Q the mutant shows no aminopeptidase activity Homo sapiens
K565A the mutant shows reduced aminopeptidase activity Homo sapiens
R563A the mutant shows no aminopeptidase activity Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ contains Zn2+ Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Arg-L-Ala-L-Arg + H2O bi-functional enzyme that also exhibits aminopeptidase activity with a preference over arginyl tripeptides Homo sapiens ?
-
 ?
leukotriene A4 + H2O
-
 Homo sapiens leukotriene B4
-
 ?

Synonyms

Synonyms Comment Organism
leukotriene A4 hydrolase
-
 Homo sapiens
LTA4H
-
 Homo sapiens