Function and Biology Details
Reactions catalysed:
(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H(2)O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate
Release of the N-terminal residue from a tripeptide.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Peptidase M1, alanine aminopeptidase/leukotriene A4 hydrolase
- Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal
- Aminopeptidase N-like , N-terminal domain superfamliy
- Aminopeptidase, leukotriene A4 hydrolase-like
- Peptidase M1, LTA-4 hydrolase/aminopeptidase, C-terminal domain superfamily
- Armadillo-type fold
- Peptidase M4/M1, CTD superfamily
- Peptidase M1, membrane alanine aminopeptidase
2 more domains
Structure analysis Details
Assembly composition:
homo trimer (preferred)
Assembly name:
Leukotriene A-4 hydrolase (preferred)
PDBe Complex ID:
PDB-CPX-140867 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leukotriene A-4 hydrolase
Molecule details ›
Chains: A, B, C
Length: 617 amino acids
Theoretical weight: 70.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 617 amino acids
Theoretical weight: 70.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P09960 (Residues: 2-611; Coverage: 100%)
Sequence domains:
Structure domains:
