leukotriene-A4 hydrolase
Identifiers
EC no.3.3.2.6
CAS no.90119-07-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins
leukotriene A4 hydrolase
Crystallographic structure of LTA4H (rainbow colored N-terminus = blue, C-terminus = red) complexed with the protease inhibitor bestatin (space-filling model, carbon = white, oxygen = red, nitrogen = blue) based on the PDB: 1HS6​ structure.
Identifiers
SymbolLTA4H
NCBI gene4048
HGNC6710
OMIM151570
PDB1SQM
RefSeqNM_000895
UniProtP09960
Other data
EC number3.3.2.6
LocusChr. 12 q22
Search for
StructuresSwiss-model
DomainsInterPro

Leukotriene A4 hydrolase, also known as LTA4H is a human gene.[1][2][3] The protein encoded by this gene is a bifunctional enzyme (EC 3.3.2.6) which converts leukotriene A4 to leukotriene B4 and acts as an aminopeptidase.[4]

Function

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.

Catalyzed reaction

The chemical reaction catalyzed by LTA4H.

Structure

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

References

  1. ^ Minami M, Ohno S, Kawasaki H, Rådmark O, Samuelsson B, Jörnvall H, Shimizu T, Seyama Y, Suzuki K (October 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 (29): 13873–6. doi:10.1016/S0021-9258(18)47872-6. PMID 3654641. Archived from the original on 2005-03-30. Retrieved 2008-09-04.
  2. ^ FFunk CD, Rådmark O, Fu JY, Matsumoto T, Jörnvall H, Shimizu T, Samuelsson B (October 1987). "Molecular cloning and amino acid sequence of leukotriene A4 hydrolase". Proc. Natl. Acad. Sci. U.S.A. 84 (19): 6677–81. Bibcode:1987PNAS...84.6677F. doi:10.1073/pnas.84.19.6677. PMC 299146. PMID 2821541.
  3. ^ Mancini JA, Evans JF (July 1995). "Cloning and characterization of the human leukotriene A4 hydrolase gene". Eur. J. Biochem. 231 (1): 65–71. doi:10.1111/j.1432-1033.1995.tb20671.x. PMID 7628486.
  4. ^ Rudberg PC, Tholander F, Andberg M, Thunnissen MM, Haeggström JZ (June 2004). "Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates". J. Biol. Chem. 279 (26): 27376–82. doi:10.1074/jbc.M401031200. PMID 15078870.

Further reading

External links


Metabolism: lipid metabolism – eicosanoid metabolism enzymes
Leukotriene signaling modulators
Hydrolases: ether bond (EC 3.3)
Enzymes
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