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Literature summary 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

Protein Variants

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.3.2.6 Zn2+ contains Zn2+ 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
-
 leukotriene B4
-
 ?

Organism

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

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
3.3.2.6 leukotriene A4 hydrolase
-
 Homo sapiens
3.3.2.6 LTA4H
-
 Homo sapiens