Leukotriene-A4 hydrolase

From Wikipedia, the free encyclopedia

In enzymology, a leukotriene-A4 hydrolase (EC 3.3.2.6) is an enzyme that catalyzes the chemical reaction

(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H₂O $\rightleftharpoons$ (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate

Thus, the two substrates of this enzyme are (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate and H₂O, whereas its product is (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate.

This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). The systematic name of this enzyme class is (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate hydrolase. Other names in common use include LTA4 hydrolase, LTA4H, and leukotriene A4 hydrolase. This enzyme participates in arachidonic acid metabolism.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1GW6, 1H19, 1HS6, and 1SQM.

[edit] References

IUBMB entry for 3.3.2.6
BRENDA references for 3.3.2.6 (Recommended.)
PubMed references for 3.3.2.6
PubMed Central references for 3.3.2.6
Google Scholar references for 3.3.2.6
Evans JF, Dupuis P, Ford-Hutchinson AW (1985). "Purification and characterisation of leukotriene A4 hydrolase from rat neutrophils". Biochim. Biophys. Acta. 840: 43–50. PMID 3995081.
Shimizu T, Seyama Y, Suzuki K (1987). "Molecular cloning of a cDNA coding for human leukotriene A4 hydrolase. Complete primary structure of an enzyme involved in eicosanoid synthesis". J. Biol. Chem. 262: 13873–6. PMID 3654641.
Haeggstrom J, Meijer J, Radmark O (1986). "Leukotriene A4. Enzymatic conversion into 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid by mouse liver cytosolic epoxide hydrolase". J. Biol. Chem. 261: 6332–7. PMID 3009453.
Newman JW, Morisseau C, Hammock BD (2005). "Epoxide hydrolases: their roles and interactions with lipid metabolism". Prog. Lipid. Res. 44: 1–51. doi:10.1016/j.plipres.2004.10.001. PMID 15748653.
Fretland AJ, Omiecinski CJ (2000). "Epoxide hydrolases: biochemistry and molecular biology". Chem. Biol. Interact. 129: 41–59. doi:10.1016/S0009-2797(00)00197-6. PMID 11154734.
Orning L, Gierse JK, Fitzpatrick FA (1994). "The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity". J. Biol. Chem. 269: 11269–73. PMID 8157657.
S, Yotsumoto H, Takaku F, Shimizu T (1987). "Leukotriene A4 hydrolase in the human lung. Inactivation of the enzyme with leukotriene A4 isomers". J. Biol. Chem. 262: 10200–5. PMID 3038871.