Leukotriene-A4 hydrolase

protein
Name=leukotriene A4 hydrolase
caption=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.


width=325px
HGNCid=6710
Symbol=LTA4H
AltSymbols=
EntrezGene=4048
OMIM=151570
RefSeq=NM_000895
UniProt=P09960
PDB=1SQM
ECnumber=3.3.2.6
Chromosome=12
Arm=q
Band=22
LocusSupplementaryData=

Leukotriene A4 hydrolase, also known as LTA4H is a human gene.cite journal | author = Minami M, Ohno S, Kawasaki H, Rådmark O, Samuelsson B, Jörnvall H, Shimizu T, Seyama Y, Suzuki K | title = Molecular cloning of a cDNA coding for human leukotriene A4 hydrolase. Complete primary structure of an enzyme involved in eicosanoid synthesis | journal = J. Biol. Chem. | volume = 262 | issue = 29 | pages = 13873–6 | year = 1987 | month = October | pmid = 3654641 | doi = | url = http://www.jbc.org/cgi/content/abstract/262/29/13873 | issn = ] cite journal | author = FFunk CD, Rådmark O, Fu JY, Matsumoto T, Jörnvall H, Shimizu T, Samuelsson B | title = Molecular cloning and amino acid sequence of leukotriene A4 hydrolase | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 84 | issue = 19 | pages = 6677–81 | year = 1987 | month = October | pmid = 2821541 | pmc = 299146 | url = http://www.pnas.org/cgi/pmidlookup?view=long&pmid=2821541 | issn = ] cite journal | author = Mancini JA, Evans JF | title = Cloning and characterization of the human leukotriene A4 hydrolase gene | journal = Eur. J. Biochem. | volume = 231 | issue = 1 | pages = 65–71 | year = 1995 | month = July | pmid = 7628486 | doi = 10.1111/j.1432-1033.1995.tb20671.x | url = | issn = ] The protein encoded by this gene a bifunctional enzyme (EC number|3.3.2.6) which converts leukotriene A4 to leukotriene B4 and acts as an aminopeptidase.cite journal | author = Rudberg PC, Tholander F, Andberg M, Thunnissen MM, Haeggström JZ | title = Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates | journal = J. Biol. Chem. | volume = 279 | issue = 26 | pages = 27376–82 | year = 2004 | month = June | pmid = 15078870 | doi = 10.1074/jbc.M401031200 | url = | issn = ]

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

tructure

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

References

Further reading

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External links

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* "The CAS registry number for this enzyme class is CAS registry|90119-07-6."
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