Leukotriene A-4 hydrolase

Details

Name
Leukotriene A-4 hydrolase
Synonyms
  • 3.3.2.6
  • Leukotriene A(4) hydrolase
  • LTA-4 hydrolase
  • LTA4
Gene Name
LTA4H
Organism
Humans
Amino acid sequence
>lcl|BSEQ0003332|Leukotriene A-4 hydrolase
MPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDL
TIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLT
PEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGETP
DPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETES
MLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISH
SWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSVKTFGET
HPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGPEIFLGFLKAYVEKFSYKSI
TTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGLPPIKPNYDMTLTNACIALSQRWITAK
EDDLNSFNATDLKDLSSHQLNEFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWL
RLCIQSKWEDAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVT
AMLVGKDLKVD
Number of residues
611
Molecular Weight
69284.64
Theoretical pI
6.1
GO Classification
Functions
aminopeptidase activity / epoxide hydrolase activity / leukotriene-A4 hydrolase activity / metalloaminopeptidase activity / peptidase activity / peptide binding / poly(A) RNA binding / zinc ion binding
Processes
arachidonic acid metabolic process / inflammatory response / leukotriene biosynthetic process / leukotriene metabolic process / peptide catabolic process / proteolysis / response to peptide hormone / response to zinc ion / small molecule metabolic process / Type I pneumocyte differentiation
Components
cytoplasm / cytosol / extracellular exosome / nucleoplasm
General Function
Zinc ion binding
Specific Function
Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0020556|Leukotriene A-4 hydrolase (LTA4H)
ATGCCCGAGATAGTGGATACCTGTTCGTTGGCCTCTCCGGCTTCCGTCTGCCGGACCAAG
CACCTGCACCTGCGCTGCAGCGTCGACTTTACTCGCCGGACGCTGACCGGGACTGCTGCT
CTCACGGTCCAGTCTCAGGAGGACAATCTGCGCAGCCTGGTTTTGGATACAAAGGACCTT
ACAATAGAAAAAGTAGTGATCAATGGACAAGAAGTCAAATATGCTCTTGGAGAAAGACAA
AGTTACAAGGGATCGCCAATGGAAATCTCTCTTCCTATCGCTTTGAGCAAAAATCAAGAA
ATTGTTATAGAAATTTCTTTTGAGACCTCTCCAAAATCTTCTGCTCTCCAGTGGCTCACT
CCTGAACAGACTTCTGGGAAGGAACACCCATATCTCTTTAGTCAGTGCCAGGCCATCCAC
TGCAGAGCAATCCTTCCTTGTCAGGACACTCCTTCTGTGAAATTAACCTATACTGCAGAG
GTGTCTGTCCCTAAAGAACTGGTGGCACTTATGAGTGCTATTCGTGATGGAGAAACACCT
GACCCAGAAGACCCAAGCAGGAAAATATACAAATTCATCCAAAAAGTTCCAATACCCTGC
TACCTGATTGCTTTAGTTGTTGGAGCTTTAGAAAGCAGGCAAATTGGCCCAAGAACTTTG
GTGTGGTCTGAGAAAGAGCAGGTGGAAAAGTCTGCTTATGAGTTTTCTGAGACTGAATCT
ATGCTTAAAATAGCAGAAGATCTGGGAGGACCGTATGTATGGGGACAGTATGACCTATTG
GTCCTGCCACCATCCTTCCCTTATGGTGGCATGGAGAATCCTTGCCTTACTTTTGTAACT
CCTACTCTACTGGCAGGCGACAAGTCACTCTCCAATGTCATTGCACATGAAATATCTCAT
AGCTGGACAGGGAATCTAGTGACCAACAAAACTTGGGATCACTTTTGGTTAAATGAGGGA
CATACTGTGTACTTGGAACGCCACATTTGCGGACGATTGTTTGGTGAAAAGTTCAGACAT
TTTAATGCTCTGGGAGGATGGGGAGAACTACAGAATTCGGTAAAGACATTTGGGGAGACA
CATCCTTTCACCAAACTTGTGGTTGATCTGACAGATATAGACCCTGATGTAGCTTATTCT
TCAGTTCCCTATGAGAAGGGCTTTGCTTTACTTTTTTACCTTGAACAACTGCTTGGAGGA
CCAGAGATTTTCCTAGGATTCTTAAAAGCTTATGTTGAGAAGTTTTCCTATAAGAGCATA
ACTACTGATGACTGGAAGGATTTCCTGTATTCCTATTTTAAAGATAAGGTTGATGTTCTC
AATCAAGTTGATTGGAATGCCTGGCTCTACTCTCCTGGACTGCCTCCCATAAAGCCCAAT
TATGATATGACTCTGACAAATGCTTGTATTGCCTTAAGTCAAAGATGGATTACTGCCAAA
GAAGATGATTTAAATTCATTCAATGCCACAGACCTGAAGGATCTCTCTTCTCATCAATTG
AATGAGTTTTTAGCACAGACGCTCCAGAGGGCACCTCTTCCATTGGGGCACATAAAGCGA
ATGCAAGAGGTGTACAACTTCAATGCCATTAACAATTCTGAAATACGATTCAGATGGCTG
CGGCTCTGCATTCAATCCAAGTGGGAGGACGCAATTCCTTTGGCGCTAAAGATGGCAACT
GAACAAGGAAGAATGAAGTTTACCCGGCCCTTATTCAAGGATCTTGCTGCCTTTGACAAA
TCCCATGATCAAGCTGTCCGAACCTACCAAGAGCACAAAGCAAGCATGCATCCCGTGACT
GCAATGCTGGTGGGGAAAGACTTAAAAGTGGATTAA
Chromosome Location
12
Locus
12q22
External Identifiers
ResourceLink
UniProtKB IDP09960
UniProtKB Entry NameLKHA4_HUMAN
GenBank Protein ID976396
GenBank Gene IDU27293
GenAtlas IDLTA4H
HGNC IDHGNC:6710
General References
  1. Minami M, Ohno S, Kawasaki H, Radmark O, Samuelsson B, Jornvall H, Shimizu T, Seyama Y, Suzuki K: Molecular cloning of a cDNA coding for human leukotriene A4 hydrolase. Complete primary structure of an enzyme involved in eicosanoid synthesis. J Biol Chem. 1987 Oct 15;262(29):13873-6. [PubMed:3654641]
  2. Funk CD, Radmark O, Fu JY, Matsumoto T, Jornvall H, Shimizu T, Samuelsson B: Molecular cloning and amino acid sequence of leukotriene A4 hydrolase. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6677-81. [PubMed:2821541]
  3. Mancini JA, Evans JF: Cloning and characterization of the human leukotriene A4 hydrolase gene. Eur J Biochem. 1995 Jul 1;231(1):65-71. [PubMed:7628486]
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  8. Odlander B, Claesson HE, Bergman T, Radmark O, Jornvall H, Haeggstrom JZ: Leukotriene A4 hydrolase in the human B-lymphocytic cell line Raji: indications of catalytically divergent forms of the enzyme. Arch Biochem Biophys. 1991 May 15;287(1):167-74. [PubMed:1897988]
  9. Radmark O, Shimizu T, Jornvall H, Samuelsson B: Leukotriene A4 hydrolase in human leukocytes. Purification and properties. J Biol Chem. 1984 Oct 25;259(20):12339-45. [PubMed:6490615]
  10. Mueller MJ, Wetterholm A, Blomster M, Jornvall H, Samuelsson B, Haeggstrom JZ: Leukotriene A4 hydrolase: mapping of a henicosapeptide involved in mechanism-based inactivation. Proc Natl Acad Sci U S A. 1995 Aug 29;92(18):8383-7. [PubMed:7667299]
  11. Jendraschak E, Kaminski WE, Kiefl R, von Schacky C: The human leukotriene A4 hydrolase gene is expressed in two alternatively spliced mRNA forms. Biochem J. 1996 Mar 15;314 ( Pt 3):733-7. [PubMed:8615763]
  12. Toh H, Minami M, Shimizu T: Molecular evolution and zinc ion binding motif of leukotriene A4 hydrolase. Biochem Biophys Res Commun. 1990 Aug 31;171(1):216-21. [PubMed:1975494]
  13. Haeggstrom JZ, Wetterholm A, Shapiro R, Vallee BL, Samuelsson B: Leukotriene A4 hydrolase: a zinc metalloenzyme. Biochem Biophys Res Commun. 1990 Nov 15;172(3):965-70. [PubMed:2244921]
  14. Medina JF, Wetterholm A, Radmark O, Shapiro R, Haeggstrom JZ, Vallee BL, Samuelsson B: Leukotriene A4 hydrolase: determination of the three zinc-binding ligands by site-directed mutagenesis and zinc analysis. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7620-4. [PubMed:1881903]
  15. Minami M, Bito H, Ohishi N, Tsuge H, Miyano M, Mori M, Wada H, Mutoh H, Shimada S, Izumi T, et al.: Leukotriene A4 hydrolase, a bifunctional enzyme. Distinction of leukotriene A4 hydrolase and aminopeptidase activities by site-directed mutagenesis at Glu-297. FEBS Lett. 1992 Sep 14;309(3):353-7. [PubMed:1516710]
  16. Wetterholm A, Medina JF, Radmark O, Shapiro R, Haeggstrom JZ, Vallee BL, Samuelsson B: Leukotriene A4 hydrolase: abrogation of the peptidase activity by mutation of glutamic acid-296. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9141-5. [PubMed:1357660]
  17. Rybina IV, Liu H, Gor Y, Feinmark SJ: Regulation of leukotriene A4 hydrolase activity in endothelial cells by phosphorylation. J Biol Chem. 1997 Dec 12;272(50):31865-71. [PubMed:9395533]
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  22. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569]
  23. Thunnissen MM, Nordlund P, Haeggstrom JZ: Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation. Nat Struct Biol. 2001 Feb;8(2):131-5. [PubMed:11175901]
  24. Thunnissen MM, Andersson B, Samuelsson B, Wong CH, Haeggstrom J: Crystal structures of leukotriene A4 hydrolase in complex with captopril and two competitive tight-binding inhibitors. FASEB J. 2002 Oct;16(12):1648-50. Epub 2002 Aug 7. [PubMed:12207002]
  25. Rudberg PC, Tholander F, Thunnissen MM, Haeggstrom JZ: Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms. J Biol Chem. 2002 Jan 11;277(2):1398-404. Epub 2001 Oct 23. [PubMed:11675384]
  26. Rudberg PC, Tholander F, Thunnissen MM, Samuelsson B, Haeggstrom JZ: Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375. Proc Natl Acad Sci U S A. 2002 Apr 2;99(7):4215-20. Epub 2002 Mar 26. [PubMed:11917124]
  27. Rudberg PC, Tholander F, Andberg M, Thunnissen MM, Haeggstrom JZ: Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates. J Biol Chem. 2004 Jun 25;279(26):27376-82. Epub 2004 Apr 12. [PubMed:15078870]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03366Imidazoleexperimental, investigationalunknownDetails
DB03424Ubenimexexperimental, investigationalunknownDetails
DB05177DG051investigationalunknownDetails
DB11781TosedostatinvestigationalunknownDetails
DB068285-[2-(1H-pyrrol-1-yl)ethoxy]-1H-indoleexperimentalunknownDetails
DB06851N-(pyridin-3-ylmethyl)anilineexperimentalunknownDetails
DB06917(4-fluorophenyl)(pyridin-4-yl)methanoneexperimentalunknownDetails
DB023523-(Benzyloxy)Pyridin-2-AmineexperimentalunknownDetails
DB070941-(2,2'-bithiophen-5-yl)methanamineexperimentalunknownDetails
DB07099N-[4-(benzyloxy)phenyl]glycinamideexperimentalunknownDetails
DB07102(2S)-2-amino-5-oxo-5-[(4-phenylmethoxyphenyl)amino]pentanoic acidexperimentalunknownDetails
DB071044-amino-N-[4-(benzyloxy)phenyl]butanamideexperimentalunknownDetails
DB07196N-methyl-1-(2-thiophen-2-ylphenyl)methanamineexperimentalunknownDetails
DB07237{4-[(2R)-pyrrolidin-2-ylmethoxy]phenyl}(4-thiophen-3-ylphenyl)methanoneexperimentalunknownDetails
DB07258(R)-pyridin-4-yl[4-(2-pyrrolidin-1-ylethoxy)phenyl]methanolexperimentalunknownDetails
DB072591-(4-thiophen-2-ylphenyl)methanamineexperimentalunknownDetails
DB07260N-benzyl-4-[(2R)-pyrrolidin-2-ylmethoxy]anilineexperimentalunknownDetails
DB072924-(2-amino-1,3-thiazol-4-yl)phenolexperimentalunknownDetails
DB02062N-[3-[(1-Aminoethyl)(Hydroxy)Phosphoryl]-2-(1,1'-Biphenyl-4-Ylmethyl)Propanoyl]AlanineexperimentalunknownDetails
DB08040N-[(2R)-2-benzyl-4-(hydroxyamino)-4-oxobutanoyl]-L-alanineexperimentalunknownDetails
DB084665-[2-(4-hydroxyphenyl)ethyl]benzene-1,3-diolexperimentalunknownDetails
DB01197CaptoprilapprovedunknowninhibitorDetails