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Leukotriene A-4 hydrolase (LTA-4 hydrolase) (EC 3.3.2.6) (Leukotriene A(4) hydrolase)

 LKHA4_HUMAN             Reviewed;         611 AA.
P09960; B4DNQ9; F8VV40; Q6IAT6; Q9UCT7;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
30-AUG-2017, entry version 212.
RecName: Full=Leukotriene A-4 hydrolase;
Short=LTA-4 hydrolase;
EC=3.3.2.6;
AltName: Full=Leukotriene A(4) hydrolase;
Name=LTA4H; Synonyms=LTA4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3654641;
Minami M., Ohno S., Kawasaki H., Raedmark O., Samuelsson B.,
Joernvall 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. 262:13873-13876(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
PubMed=2821541; DOI=10.1073/pnas.84.19.6677;
Funk C.D., Raadmark O., Fu J.Y., Matsumoto T., Joernvall H.,
Shimizu T., Samuelsson B.;
"Molecular cloning and amino acid sequence of leukotriene A4
hydrolase.";
Proc. Natl. Acad. Sci. U.S.A. 84:6677-6681(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7628486; DOI=10.1111/j.1432-1033.1995.tb20671.x;
Mancini J.A., Evans J.F.;
"Cloning and characterization of the human leukotriene A4 hydrolase
gene.";
Eur. J. Biochem. 231:65-71(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Lung;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Esophageal carcinoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 2-22, FUNCTION, AND CATALYTIC ACTIVITY.
TISSUE=B-cell;
PubMed=1897988; DOI=10.1016/0003-9861(91)90402-5;
Odlander B., Claesson H.E., Bergman T., Radmark O., Joernvall H.,
Haeggstrom J.Z.;
"Leukotriene A4 hydrolase in the human B-lymphocytic cell line Raji:
indications of catalytically divergent forms of the enzyme.";
Arch. Biochem. Biophys. 287:167-174(1991).
[11]
PROTEIN SEQUENCE OF 2-16.
PubMed=6490615;
Radmark O., Shimizu T., Joernvall H., Samuelsson B.;
"Leukotriene A4 hydrolase in human leukocytes. Purification and
properties.";
J. Biol. Chem. 259:12339-12345(1984).
[12]
PROTEIN SEQUENCE OF 366-386, ENZYME REGULATION, COVALENT MODIFICATION
AT TYR-379, AND CATALYTIC ACTIVITY.
PubMed=7667299; DOI=10.1073/pnas.92.18.8383;
Mueller M.J., Wetterholm A., Blomster M., Jornvall H., Samuelsson B.,
Haeggstrom J.Z.;
"Leukotriene A4 hydrolase: mapping of a henicosapeptide involved in
mechanism-based inactivation.";
Proc. Natl. Acad. Sci. U.S.A. 92:8383-8387(1995).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 511-611, AND ALTERNATIVE SPLICING
(ISOFORMS 1 AND 2).
PubMed=8615763; DOI=10.1042/bj3140733;
Jendraschak E., Kaminski W.E., Kiefl R., von Schacky C.;
"The human leukotriene A4 hydrolase gene is expressed in two
alternatively spliced mRNA forms.";
Biochem. J. 314:733-737(1996).
[14]
ZINC-BINDING, FUNCTION AS A PEPTIDASE, AND SIMILARITY TO ZINC
PROTEASES.
PubMed=1975494; DOI=10.1016/0006-291X(90)91379-7;
Toh H., Minami M., Shimizu T.;
"Molecular evolution and zinc ion binding motif of leukotriene A4
hydrolase.";
Biochem. Biophys. Res. Commun. 171:216-221(1990).
[15]
ZINC-BINDING, AND FUNCTION AS A PEPTIDASE.
PubMed=2244921; DOI=10.1016/0006-291X(90)91540-9;
Haeggstroem J.Z., Wetterholm A., Shapiro R., Vallee B.L.,
Samuelsson B.;
"Leukotriene A4 hydrolase: a zinc metalloenzyme.";
Biochem. Biophys. Res. Commun. 172:965-970(1990).
[16]
MUTAGENESIS OF ZINC LIGANDS.
PubMed=1881903; DOI=10.1073/pnas.88.17.7620;
Medina J.F., Wetterholm A., Raadmark O., Shapiro R., Haeggstroem J.Z.,
Vallee B.L., 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. 88:7620-7624(1991).
[17]
MUTAGENESIS OF GLU-297.
PubMed=1516710; DOI=10.1016/0014-5793(92)80806-R;
Minami M., Bito H., Ohishi N., Tsuge H., Miyano M., Mori M., Wada H.,
Mutoh H., Shimada S., Izumi T., Abe K., Shimuzu T.;
"Leukotriene A4 hydrolase, a bifunctional enzyme. Distinction of
leukotriene A4 hydrolase and aminopeptidase activities by site-
directed mutagenesis at Glu-297.";
FEBS Lett. 309:353-357(1992).
[18]
MUTAGENESIS OF GLU-297.
PubMed=1357660; DOI=10.1073/pnas.89.19.9141;
Wetterholm A., Medina J.F., Raadmark O., Shapiro R., Haeggstroem J.Z.,
Vallee B.L., Samuelsson B.;
"Leukotriene A4 hydrolase: abrogation of the peptidase activity by
mutation of glutamic acid-296.";
Proc. Natl. Acad. Sci. U.S.A. 89:9141-9145(1992).
[19]
PHOSPHORYLATION AT SER-416.
PubMed=9395533; DOI=10.1074/jbc.272.50.31865;
Rybina I.V., Liu H., Gor Y., Feinmark S.J.;
"Regulation of leukotriene A4 hydrolase activity in endothelial cells
by phosphorylation.";
J. Biol. Chem. 272:31865-31871(1997).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-337; LYS-414 AND
LYS-573, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
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 96:253-262(2014).
[25]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ZINC AND
BESTATIN.
PubMed=11175901; DOI=10.1038/84117;
Thunnissen M.M.G.M., Nordlund P., Haeggstroem J.Z.;
"Crystal structure of human leukotriene A(4) hydrolase, a bifunctional
enzyme in inflammation.";
Nat. Struct. Biol. 8:131-135(2001).
[26]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH CAPTOPRIL AND
ZINC IONS, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, AND ACTIVE SITE.
PubMed=12207002; DOI=10.1096/fj.01-1017fje;
Thunnissen M.M., Andersson B., Samuelsson B., Wong C.H.,
Haeggstrom J.Z.;
"Crystal structures of leukotriene A4 hydrolase in complex with
captopril and two competitive tight-binding inhibitors.";
FASEB J. 16:1648-1650(2002).
[27]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-611 IN COMPLEX WITH ZINC,
ACTIVE SITE, AND MUTAGENESIS OF GLN-137; GLY-270; MET-271; GLU-272 AND
ASN-273.
PubMed=11675384; DOI=10.1074/jbc.M106577200;
Rudberg P.C., Tholander F., Thunnissen M.M.G.M., Haeggstroem J.Z.;
"Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic
residue with specific roles in two distinct enzyme mechanisms.";
J. Biol. Chem. 277:1398-1404(2002).
[28]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT ASN-376 IN COMPLEX
WITH BESTATIN AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, AND
MUTAGENESIS OF GLN-135; HIS-140; ASP-372; ASP-374; ASP-376 AND
GLU-385.
PubMed=11917124; DOI=10.1073/pnas.072090099;
Rudberg P.C., Tholander F., Thunnissen M.M., Samuelsson B.,
Haeggstrom J.Z.;
"Leukotriene A4 hydrolase: selective abrogation of leukotriene B4
formation by mutation of aspartic acid 375.";
Proc. Natl. Acad. Sci. U.S.A. 99:4215-4220(2002).
[29]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ALA-564 IN COMPLEX
WITH ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, AND
MUTAGENESIS OF ARG-564 AND LYS-566.
PubMed=15078870; DOI=10.1074/jbc.M401031200;
Rudberg P.C., Tholander F., Andberg M., Thunnissen M.M.,
Haeggstrom J.Z.;
"Leukotriene A4 hydrolase: identification of a common carboxylate
recognition site for the epoxide hydrolase and aminopeptidase
substrates.";
J. Biol. Chem. 279:27376-27382(2004).
[30]
X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF MUTANT GLN-297 IN COMPLEXES
WITH SUBSTRATE TRIPEPTIDES AND ZINC IONS, CATALYTIC ACTIVITY,
FUNCTION, COFACTOR, AND MUTAGENESIS OF GLU-297 AND ASP-376.
PubMed=18804029; DOI=10.1016/j.chembiol.2008.07.018;
Tholander F., Muroya A., Roques B.P., Fournie-Zaluski M.C.,
Thunnissen M.M., Haeggstrom J.Z.;
"Structure-based dissection of the active site chemistry of
leukotriene A4 hydrolase: implications for M1 aminopeptidases and
inhibitor design.";
Chem. Biol. 15:920-929(2008).
[31]
X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) IN COMPLEXES WITH INHIBITORS
AND ZINC IONS.
PubMed=19618939; DOI=10.1021/jm900259h;
Davies D.R., Mamat B., Magnusson O.T., Christensen J.,
Haraldsson M.H., Mishra R., Pease B., Hansen E., Singh J.,
Zembower D., Kim H., Kiselyov A.S., Burgin A.B., Gurney M.E.,
Stewart L.J.;
"Discovery of leukotriene A4 hydrolase inhibitors using metabolomics
biased fragment crystallography.";
J. Med. Chem. 52:4694-4715(2009).
-!- FUNCTION: Epoxide hydrolase that catalyzes the final step in the
biosynthesis of the proinflammatory mediator leukotriene B4. Has
also aminopeptidase activity. {ECO:0000269|PubMed:11917124,
ECO:0000269|PubMed:12207002, ECO:0000269|PubMed:15078870,
ECO:0000269|PubMed:18804029, ECO:0000269|PubMed:1897988,
ECO:0000269|PubMed:1975494, ECO:0000269|PubMed:2244921}.
-!- CATALYTIC ACTIVITY: (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.
{ECO:0000269|PubMed:11917124, ECO:0000269|PubMed:12207002,
ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:18804029,
ECO:0000269|PubMed:1897988, ECO:0000269|PubMed:7667299}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:12207002,
ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:18804029};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12207002,
ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:18804029};
-!- ENZYME REGULATION: Inhibited by bestatin. Subject to suicide
inhibition by leukotriene A4, due to the formation of a covalent
adduct at Tyr-379. {ECO:0000269|PubMed:7667299}.
-!- PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11917124,
ECO:0000269|PubMed:12207002, ECO:0000269|PubMed:15078870}.
-!- INTERACTION:
Q9BSI4:TINF2; NbExp=2; IntAct=EBI-721089, EBI-717399;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=L-LTA4;
IsoId=P09960-1; Sequence=Displayed;
Name=2; Synonyms=S-LTA4;
IsoId=P09960-2; Sequence=VSP_041108, VSP_041109;
Name=3;
IsoId=P09960-3; Sequence=VSP_041107, VSP_041108, VSP_041109;
Name=4;
IsoId=P09960-4; Sequence=VSP_041107;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in
monocytes, lymphocytes, neutrophils, reticulocytes, platelets and
fibroblasts.
-!- PTM: Phosphorylation at Ser-416 inhibits enzymatic activity.
{ECO:0000269|PubMed:9395533}.
-!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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EMBL; J03459; AAA36176.1; -; mRNA.
EMBL; J02959; AAA36177.1; -; mRNA.
EMBL; U27293; AAA89077.1; -; Genomic_DNA.
EMBL; U27275; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27276; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27277; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27278; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27279; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27280; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27281; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27282; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27283; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27284; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27285; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27286; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27287; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27288; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27289; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27290; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27291; AAA89077.1; JOINED; Genomic_DNA.
EMBL; U27292; AAA89077.1; JOINED; Genomic_DNA.
EMBL; AK298017; BAG60321.1; -; mRNA.
EMBL; CR457068; CAG33349.1; -; mRNA.
EMBL; BX647158; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC007298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW97559.1; -; Genomic_DNA.
EMBL; BC032528; AAH32528.1; -; mRNA.
EMBL; U43410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U43411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS58266.1; -. [P09960-3]
CCDS; CCDS58267.1; -. [P09960-4]
CCDS; CCDS9059.1; -. [P09960-1]
PIR; S65947; S65947.
RefSeq; NP_000886.1; NM_000895.2. [P09960-1]
RefSeq; NP_001243572.1; NM_001256643.1. [P09960-4]
RefSeq; NP_001243573.1; NM_001256644.1. [P09960-3]
RefSeq; XP_005268928.1; XM_005268871.1. [P09960-2]
UniGene; Hs.524648; -.
PDB; 1GW6; X-ray; 2.20 A; A=2-611.
PDB; 1H19; X-ray; 2.10 A; A=2-611.
PDB; 1HS6; X-ray; 1.95 A; A=1-611.
PDB; 1SQM; X-ray; 2.30 A; A=2-611.
PDB; 2R59; X-ray; 1.89 A; A=2-611.
PDB; 2VJ8; X-ray; 1.80 A; A=1-611.
PDB; 3B7R; X-ray; 1.81 A; L=2-611.
PDB; 3B7S; X-ray; 1.47 A; A=2-611.
PDB; 3B7T; X-ray; 2.30 A; A=2-611.
PDB; 3B7U; X-ray; 1.90 A; X=2-611.
PDB; 3CHO; X-ray; 1.80 A; A=2-611.
PDB; 3CHP; X-ray; 2.10 A; A=2-611.
PDB; 3CHQ; X-ray; 2.09 A; A=2-611.
PDB; 3CHR; X-ray; 2.20 A; A=2-611.
PDB; 3CHS; X-ray; 2.55 A; A=2-611.
PDB; 3FH5; X-ray; 1.63 A; A=1-611.
PDB; 3FH7; X-ray; 2.05 A; A=1-611.
PDB; 3FH8; X-ray; 1.67 A; A=1-611.
PDB; 3FHE; X-ray; 2.16 A; A=1-611.
PDB; 3FTS; X-ray; 2.33 A; A=1-611.
PDB; 3FTU; X-ray; 1.90 A; A=1-611.
PDB; 3FTV; X-ray; 1.70 A; A=1-611.
PDB; 3FTW; X-ray; 1.85 A; A=1-611.
PDB; 3FTX; X-ray; 1.96 A; A=1-611.
PDB; 3FTY; X-ray; 2.15 A; A=1-611.
PDB; 3FTZ; X-ray; 2.00 A; A=1-611.
PDB; 3FU0; X-ray; 1.80 A; A=1-611.
PDB; 3FU3; X-ray; 2.00 A; A=1-611.
PDB; 3FU5; X-ray; 2.30 A; A=1-611.
PDB; 3FU6; X-ray; 2.05 A; A=1-611.
PDB; 3FUD; X-ray; 2.20 A; A=1-611.
PDB; 3FUE; X-ray; 2.38 A; A=1-611.
PDB; 3FUF; X-ray; 2.60 A; A=1-611.
PDB; 3FUH; X-ray; 1.80 A; A=1-611.
PDB; 3FUI; X-ray; 2.20 A; A=1-611.
PDB; 3FUJ; X-ray; 1.90 A; A=1-611.
PDB; 3FUK; X-ray; 1.95 A; A=1-611.
PDB; 3FUL; X-ray; 2.39 A; A=1-611.
PDB; 3FUM; X-ray; 2.15 A; A=1-611.
PDB; 3FUN; X-ray; 1.58 A; A=1-611.
PDB; 3U9W; X-ray; 1.25 A; A=4-611.
PDB; 4DPR; X-ray; 2.02 A; A=1-611.
PDB; 4L2L; X-ray; 1.65 A; A=1-611.
PDB; 4MKT; X-ray; 1.62 A; A=1-611.
PDB; 4MS6; X-ray; 1.72 A; A=1-611.
PDB; 4R7L; X-ray; 1.66 A; A=1-611.
PDB; 4RSY; X-ray; 1.93 A; A=1-611.
PDB; 4RVB; X-ray; 1.93 A; A=1-611.
PDB; 5AEN; X-ray; 1.86 A; A=4-611.
PDB; 5BPP; X-ray; 2.03 A; A=1-611.
PDB; 5FWQ; X-ray; 2.05 A; A=1-611.
PDB; 5N3W; X-ray; 2.30 A; A=1-611.
PDBsum; 1GW6; -.
PDBsum; 1H19; -.
PDBsum; 1HS6; -.
PDBsum; 1SQM; -.
PDBsum; 2R59; -.
PDBsum; 2VJ8; -.
PDBsum; 3B7R; -.
PDBsum; 3B7S; -.
PDBsum; 3B7T; -.
PDBsum; 3B7U; -.
PDBsum; 3CHO; -.
PDBsum; 3CHP; -.
PDBsum; 3CHQ; -.
PDBsum; 3CHR; -.
PDBsum; 3CHS; -.
PDBsum; 3FH5; -.
PDBsum; 3FH7; -.
PDBsum; 3FH8; -.
PDBsum; 3FHE; -.
PDBsum; 3FTS; -.
PDBsum; 3FTU; -.
PDBsum; 3FTV; -.
PDBsum; 3FTW; -.
PDBsum; 3FTX; -.
PDBsum; 3FTY; -.
PDBsum; 3FTZ; -.
PDBsum; 3FU0; -.
PDBsum; 3FU3; -.
PDBsum; 3FU5; -.
PDBsum; 3FU6; -.
PDBsum; 3FUD; -.
PDBsum; 3FUE; -.
PDBsum; 3FUF; -.
PDBsum; 3FUH; -.
PDBsum; 3FUI; -.
PDBsum; 3FUJ; -.
PDBsum; 3FUK; -.
PDBsum; 3FUL; -.
PDBsum; 3FUM; -.
PDBsum; 3FUN; -.
PDBsum; 3U9W; -.
PDBsum; 4DPR; -.
PDBsum; 4L2L; -.
PDBsum; 4MKT; -.
PDBsum; 4MS6; -.
PDBsum; 4R7L; -.
PDBsum; 4RSY; -.
PDBsum; 4RVB; -.
PDBsum; 5AEN; -.
PDBsum; 5BPP; -.
PDBsum; 5FWQ; -.
PDBsum; 5N3W; -.
ProteinModelPortal; P09960; -.
SMR; P09960; -.
BioGrid; 110226; 23.
IntAct; P09960; 7.
MINT; MINT-1388946; -.
STRING; 9606.ENSP00000228740; -.
BindingDB; P09960; -.
ChEMBL; CHEMBL4618; -.
DrugBank; DB07102; (2S)-2-amino-5-oxo-5-[(4-phenylmethoxyphenyl)amino]pentanoic acid.
DrugBank; DB06917; (4-fluorophenyl)(pyridin-4-yl)methanone.
DrugBank; DB07258; (R)-pyridin-4-yl[4-(2-pyrrolidin-1-ylethoxy)phenyl]methanol.
DrugBank; DB07259; 1-(4-thiophen-2-ylphenyl)methanamine.
DrugBank; DB02352; 3-(Benzyloxy)Pyridin-2-Amine.
DrugBank; DB07104; 4-amino-N-[4-(benzyloxy)phenyl]butanamide.
DrugBank; DB06828; 5-[2-(1H-pyrrol-1-yl)ethoxy]-1H-indole.
DrugBank; DB01197; Captopril.
DrugBank; DB05745; CHR-2797.
DrugBank; DB05177; DG051.
DrugBank; DB06851; N-(pyridin-3-ylmethyl)aniline.
DrugBank; DB08040; N-[(2R)-2-benzyl-4-(hydroxyamino)-4-oxobutanoyl]-L-alanine.
DrugBank; DB07099; N-[4-(benzyloxy)phenyl]glycinamide.
DrugBank; DB07260; N-benzyl-4-[(2R)-pyrrolidin-2-ylmethoxy]aniline.
DrugBank; DB07196; N-methyl-1-(2-thiophen-2-ylphenyl)methanamine.
DrugBank; DB03424; Ubenimex.
DrugBank; DB07237; {4-[(2R)-pyrrolidin-2-ylmethoxy]phenyl}(4-thiophen-3-ylphenyl)methanone.
GuidetoPHARMACOLOGY; 1395; -.
SwissLipids; SLP:000001118; -.
MEROPS; M01.004; -.
iPTMnet; P09960; -.
PhosphoSitePlus; P09960; -.
SwissPalm; P09960; -.
BioMuta; LTA4H; -.
DMDM; 126353; -.
REPRODUCTION-2DPAGE; IPI00219077; -.
EPD; P09960; -.
MaxQB; P09960; -.
PaxDb; P09960; -.
PeptideAtlas; P09960; -.
PRIDE; P09960; -.
DNASU; 4048; -.
Ensembl; ENST00000228740; ENSP00000228740; ENSG00000111144. [P09960-1]
Ensembl; ENST00000413268; ENSP00000395051; ENSG00000111144. [P09960-3]
Ensembl; ENST00000552789; ENSP00000449958; ENSG00000111144. [P09960-4]
GeneID; 4048; -.
KEGG; hsa:4048; -.
UCSC; uc001ten.3; human. [P09960-1]
CTD; 4048; -.
DisGeNET; 4048; -.
GeneCards; LTA4H; -.
HGNC; HGNC:6710; LTA4H.
HPA; CAB015221; -.
HPA; HPA008399; -.
HPA; HPA017017; -.
MIM; 151570; gene.
neXtProt; NX_P09960; -.
OpenTargets; ENSG00000111144; -.
PharmGKB; PA24345; -.
eggNOG; KOG1047; Eukaryota.
eggNOG; COG0308; LUCA.
GeneTree; ENSGT00530000063003; -.
HOGENOM; HOG000293296; -.
HOVERGEN; HBG001274; -.
InParanoid; P09960; -.
KO; K01254; -.
OMA; NFEHFWL; -.
OrthoDB; EOG091G02UX; -.
PhylomeDB; P09960; -.
TreeFam; TF300758; -.
BioCyc; MetaCyc:HS03372-MONOMER; -.
BRENDA; 3.3.2.6; 2681.
Reactome; R-HSA-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-HSA-6798695; Neutrophil degranulation.
SABIO-RK; P09960; -.
UniPathway; UPA00878; -.
ChiTaRS; LTA4H; human.
EvolutionaryTrace; P09960; -.
GenomeRNAi; 4048; -.
PRO; PR:P09960; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111144; -.
CleanEx; HS_LTA4H; -.
ExpressionAtlas; P09960; baseline and differential.
Genevisible; P09960; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
GO; GO:0004301; F:epoxide hydrolase activity; IDA:UniProtKB.
GO; GO:0004463; F:leukotriene-A4 hydrolase activity; IDA:UniProtKB.
GO; GO:0070006; F:metalloaminopeptidase activity; IMP:CAFA.
GO; GO:0008233; F:peptidase activity; TAS:ProtInc.
GO; GO:0042277; F:peptide binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
GO; GO:0044267; P:cellular protein metabolic process; IMP:CAFA.
GO; GO:0019370; P:leukotriene biosynthetic process; IDA:UniProtKB.
GO; GO:0006691; P:leukotriene metabolic process; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0043171; P:peptide catabolic process; IDA:UniProtKB.
CDD; cd09599; M1_LTA4H; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR012777; Leukotriene_A4_hydrolase.
InterPro; IPR034015; M1_LTA4H.
InterPro; IPR001930; Peptidase_M1.
InterPro; IPR015211; Peptidase_M1_C.
InterPro; IPR014782; Peptidase_M1_N.
PANTHER; PTHR11533; PTHR11533; 1.
Pfam; PF09127; Leuk-A4-hydro_C; 1.
Pfam; PF01433; Peptidase_M1; 1.
PRINTS; PR00756; ALADIPTASE.
SMART; SM01263; Leuk-A4-hydro_C; 1.
SUPFAM; SSF48371; SSF48371; 1.
TIGRFAMs; TIGR02411; leuko_A4_hydro; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Hydrolase;
Leukotriene biosynthesis; Metal-binding; Metalloprotease;
Phosphoprotein; Polymorphism; Protease; Reference proteome; Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000269|PubMed:1897988,
ECO:0000269|PubMed:6490615}.
CHAIN 2 611 Leukotriene A-4 hydrolase.
/FTId=PRO_0000095124.
REGION 135 137 Substrate binding.
{ECO:0000269|PubMed:18804029}.
REGION 267 272 Substrate binding.
{ECO:0000269|PubMed:18804029}.
REGION 564 566 Substrate binding.
{ECO:0000269|PubMed:18804029}.
ACT_SITE 297 297 Proton acceptor. {ECO:0000244|PDB:1H19,
ECO:0000269|PubMed:11675384,
ECO:0000305|PubMed:12207002}.
ACT_SITE 384 384 Proton donor. {ECO:0000244|PDB:1H19,
ECO:0000269|PubMed:11675384,
ECO:0000305|PubMed:12207002}.
METAL 296 296 Zinc; catalytic. {ECO:0000244|PDB:1GW6,
ECO:0000244|PDB:1H19,
ECO:0000244|PDB:1HS6,
ECO:0000244|PDB:1SQM,
ECO:0000244|PDB:2R59,
ECO:0000244|PDB:2VJ8,
ECO:0000244|PDB:3B7R,
ECO:0000244|PDB:3B7S,
ECO:0000244|PDB:3B7T,
ECO:0000244|PDB:3B7U,
ECO:0000244|PDB:3CHO,
ECO:0000244|PDB:3CHP,
ECO:0000244|PDB:3CHQ,
ECO:0000244|PDB:3CHR,
ECO:0000244|PDB:3CHS,
ECO:0000244|PDB:3FH5,
ECO:0000244|PDB:3FH7,
ECO:0000244|PDB:3FH8,
ECO:0000244|PDB:3FHE,
ECO:0000244|PDB:3FTS,
ECO:0000244|PDB:3FTU,
ECO:0000244|PDB:3FTV,
ECO:0000244|PDB:3FTW,
ECO:0000244|PDB:3FTX,
ECO:0000244|PDB:3FTY,
ECO:0000244|PDB:3FTZ,
ECO:0000244|PDB:3FU0,
ECO:0000244|PDB:3FU3,
ECO:0000244|PDB:3FU5,
ECO:0000244|PDB:3FU6,
ECO:0000244|PDB:3FUD,
ECO:0000244|PDB:3FUE,
ECO:0000244|PDB:3FUF,
ECO:0000244|PDB:3FUH,
ECO:0000244|PDB:3FUI,
ECO:0000244|PDB:3FUJ,
ECO:0000244|PDB:3FUK,
ECO:0000244|PDB:3FUL,
ECO:0000244|PDB:3FUM,
ECO:0000244|PDB:3FUN,
ECO:0000244|PDB:3U9W,
ECO:0000244|PDB:4DPR,
ECO:0000244|PDB:4L2L,
ECO:0000244|PDB:4MKT,
ECO:0000244|PDB:4MS6,
ECO:0000244|PDB:5AEN,
ECO:0000269|PubMed:11175901,
ECO:0000269|PubMed:11675384,
ECO:0000269|PubMed:11917124,
ECO:0000269|PubMed:12207002,
ECO:0000269|PubMed:15078870,
ECO:0000269|PubMed:18804029,
ECO:0000269|PubMed:19618939}.
METAL 300 300 Zinc; catalytic. {ECO:0000244|PDB:1GW6,
ECO:0000244|PDB:1H19,
ECO:0000244|PDB:1HS6,
ECO:0000244|PDB:1SQM,
ECO:0000244|PDB:2R59,
ECO:0000244|PDB:2VJ8,
ECO:0000244|PDB:3B7R,
ECO:0000244|PDB:3B7S,
ECO:0000244|PDB:3B7T,
ECO:0000244|PDB:3B7U,
ECO:0000244|PDB:3CHO,
ECO:0000244|PDB:3CHP,
ECO:0000244|PDB:3CHQ,
ECO:0000244|PDB:3CHR,
ECO:0000244|PDB:3CHS,
ECO:0000244|PDB:3FH5,
ECO:0000244|PDB:3FH7,
ECO:0000244|PDB:3FH8,
ECO:0000244|PDB:3FHE,
ECO:0000244|PDB:3FTS,
ECO:0000244|PDB:3FTU,
ECO:0000244|PDB:3FTV,
ECO:0000244|PDB:3FTW,
ECO:0000244|PDB:3FTX,
ECO:0000244|PDB:3FTY,
ECO:0000244|PDB:3FTZ,
ECO:0000244|PDB:3FU0,
ECO:0000244|PDB:3FU3,
ECO:0000244|PDB:3FU5,
ECO:0000244|PDB:3FU6,
ECO:0000244|PDB:3FUD,
ECO:0000244|PDB:3FUE,
ECO:0000244|PDB:3FUF,
ECO:0000244|PDB:3FUH,
ECO:0000244|PDB:3FUI,
ECO:0000244|PDB:3FUJ,
ECO:0000244|PDB:3FUK,
ECO:0000244|PDB:3FUL,
ECO:0000244|PDB:3FUM,
ECO:0000244|PDB:3FUN,
ECO:0000244|PDB:3U9W,
ECO:0000244|PDB:4DPR,
ECO:0000244|PDB:4L2L,
ECO:0000244|PDB:4MKT,
ECO:0000244|PDB:4MS6,
ECO:0000244|PDB:5AEN,
ECO:0000269|PubMed:11175901,
ECO:0000269|PubMed:11675384,
ECO:0000269|PubMed:11917124,
ECO:0000269|PubMed:12207002,
ECO:0000269|PubMed:15078870,
ECO:0000269|PubMed:18804029,
ECO:0000269|PubMed:19618939}.
METAL 319 319 Zinc; catalytic. {ECO:0000244|PDB:1GW6,
ECO:0000244|PDB:1H19,
ECO:0000244|PDB:1HS6,
ECO:0000244|PDB:1SQM,
ECO:0000244|PDB:2R59,
ECO:0000244|PDB:2VJ8,
ECO:0000244|PDB:3B7R,
ECO:0000244|PDB:3B7S,
ECO:0000244|PDB:3B7T,
ECO:0000244|PDB:3B7U,
ECO:0000244|PDB:3CHO,
ECO:0000244|PDB:3CHP,
ECO:0000244|PDB:3CHQ,
ECO:0000244|PDB:3CHR,
ECO:0000244|PDB:3CHS,
ECO:0000244|PDB:3FH5,
ECO:0000244|PDB:3FH7,
ECO:0000244|PDB:3FH8,
ECO:0000244|PDB:3FHE,
ECO:0000244|PDB:3FTS,
ECO:0000244|PDB:3FTU,
ECO:0000244|PDB:3FTV,
ECO:0000244|PDB:3FTW,
ECO:0000244|PDB:3FTX,
ECO:0000244|PDB:3FTY,
ECO:0000244|PDB:3FTZ,
ECO:0000244|PDB:3FU0,
ECO:0000244|PDB:3FU3,
ECO:0000244|PDB:3FU5,
ECO:0000244|PDB:3FU6,
ECO:0000244|PDB:3FUD,
ECO:0000244|PDB:3FUE,
ECO:0000244|PDB:3FUF,
ECO:0000244|PDB:3FUH,
ECO:0000244|PDB:3FUI,
ECO:0000244|PDB:3FUJ,
ECO:0000244|PDB:3FUK,
ECO:0000244|PDB:3FUL,
ECO:0000244|PDB:3FUM,
ECO:0000244|PDB:3FUN,
ECO:0000244|PDB:3U9W,
ECO:0000244|PDB:4DPR,
ECO:0000244|PDB:4L2L,
ECO:0000244|PDB:4MKT,
ECO:0000244|PDB:4MS6,
ECO:0000244|PDB:5AEN,
ECO:0000269|PubMed:11175901,
ECO:0000269|PubMed:11675384,
ECO:0000269|PubMed:11917124,
ECO:0000269|PubMed:12207002,
ECO:0000269|PubMed:15078870,
ECO:0000269|PubMed:18804029,
ECO:0000269|PubMed:19618939}.
SITE 376 376 Essential for epoxide hydrolase activity,
but not for aminopeptidase activity.
SITE 379 379 Covalently modified during suicide
inhibition by leukotrienes.
MOD_RES 73 73 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 337 337 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 414 414 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 416 416 Phosphoserine.
{ECO:0000269|PubMed:9395533}.
MOD_RES 573 573 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 53 MPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAAL
TVQSQEDNLRSL -> MLPQRNLSKRQVPTMHIPVKTRRLL
AALK (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_041107.
VAR_SEQ 511 532 APLPLGHIKRMQEVYNFNAINN -> MAAALHSIQVGGRNS
FGAKDGN (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041108.
VAR_SEQ 533 611 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041109.
VARIANT 131 131 Y -> H (in dbSNP:rs45630737).
/FTId=VAR_051570.
MUTAGEN 135 135 Q->A,L: Srongly increased epoxide
hydrolase activity.
{ECO:0000269|PubMed:11917124}.
MUTAGEN 135 135 Q->A: Strongly reduced aminopeptidase
activity. Strongly decreased affinity for
leukotriene. Abolishes epoxide hydrolase
activity. {ECO:0000269|PubMed:11917124}.
MUTAGEN 137 137 Q->A: No loss of activity.
{ECO:0000269|PubMed:11675384}.
MUTAGEN 137 137 Q->L: Aminopeptidase activity strongly
impaired, but keeps LTA4 activity.
{ECO:0000269|PubMed:11675384}.
MUTAGEN 137 137 Q->N: Aminopeptidase activity almost
absent, but keeps LTA4 activity.
{ECO:0000269|PubMed:11675384}.
MUTAGEN 140 140 H->Q: Aminopeptidase activity almost
absent, but keeps LTA4 activity.
{ECO:0000269|PubMed:11917124}.
MUTAGEN 269 269 G->A: No loss of activity.
{ECO:0000269|PubMed:1881903}.
MUTAGEN 270 270 G->A: No loss of activity.
{ECO:0000269|PubMed:11675384}.
MUTAGEN 271 271 M->L: No loss of activity.
{ECO:0000269|PubMed:11675384}.
MUTAGEN 272 272 E->A,D: Complete loss of activity.
{ECO:0000269|PubMed:11675384}.
MUTAGEN 272 272 E->Q: Loss of LTA4 activity, and
aminopeptidase activity strongly
impaired. {ECO:0000269|PubMed:11675384}.
MUTAGEN 273 273 N->A: No loss of activity.
{ECO:0000269|PubMed:11675384}.
MUTAGEN 296 296 H->Y: Complete loss of activity.
{ECO:0000269|PubMed:1881903}.
MUTAGEN 297 297 E->A: Loss of both activities.
{ECO:0000269|PubMed:1357660,
ECO:0000269|PubMed:1516710,
ECO:0000269|PubMed:18804029}.
MUTAGEN 297 297 E->K: Loss of both activities.
{ECO:0000269|PubMed:1357660,
ECO:0000269|PubMed:1516710,
ECO:0000269|PubMed:18804029}.
MUTAGEN 297 297 E->Q: Loss of aminopeptidase activity,
but keeps LTA4 activity.
{ECO:0000269|PubMed:1357660,
ECO:0000269|PubMed:1516710,
ECO:0000269|PubMed:18804029}.
MUTAGEN 300 300 H->L: Complete loss of activity.
{ECO:0000269|PubMed:1881903}.
MUTAGEN 319 319 E->A: Complete loss of activity.
{ECO:0000269|PubMed:1881903}.
MUTAGEN 372 372 D->N: No loss of activity.
{ECO:0000269|PubMed:11917124}.
MUTAGEN 374 374 D->N: No loss of activity.
{ECO:0000269|PubMed:11917124}.
MUTAGEN 376 376 D->A: Strongly reduced hydrolysis of
peptides starting with Arg. Small effect
on hydrolysis of peptides starting with
Ala. Strongly reduced epoxide hydrolase
activity. {ECO:0000269|PubMed:11917124,
ECO:0000269|PubMed:18804029}.
MUTAGEN 376 376 D->E: Strongly reduced aminopeptidase
activity. Abolishes epoxide hydrolase
activity. {ECO:0000269|PubMed:11917124,
ECO:0000269|PubMed:18804029}.
MUTAGEN 376 376 D->N: Abolishes aminopeptidase and
epoxide hydrolase activity.
{ECO:0000269|PubMed:11917124,
ECO:0000269|PubMed:18804029}.
MUTAGEN 385 385 E->Q: Reduced aminopeptidase activity.
Minor effect on epoxide hydrolase
activity. {ECO:0000269|PubMed:11917124}.
MUTAGEN 564 564 R->A,K,M: Abolishes epoxide hydrolase
activity. Reduced aminopeptidase
activity. {ECO:0000269|PubMed:15078870}.
MUTAGEN 566 566 K->A,M: Strongly reduced affinity for
peptide substrates. Reduced epoxide
hydrolase and aminopeptidase activity.
{ECO:0000269|PubMed:15078870}.
MUTAGEN 566 566 K->R: No effect on epoxide hydrolase and
aminopeptidase activity.
{ECO:0000269|PubMed:15078870}.
CONFLICT 115 115 A -> T (in Ref. 6; BX647158).
{ECO:0000305}.
CONFLICT 123 123 Q -> R (in Ref. 6; BX647158).
{ECO:0000305}.
CONFLICT 297 297 E -> G (in Ref. 4; BAG60321).
{ECO:0000305}.
CONFLICT 309 309 N -> S (in Ref. 6; BX647158).
{ECO:0000305}.
CONFLICT 378 378 A -> V (in Ref. 6; BX647158).
{ECO:0000305}.
TURN 14 16 {ECO:0000244|PDB:3U9W}.
STRAND 17 29 {ECO:0000244|PDB:3U9W}.
TURN 30 33 {ECO:0000244|PDB:3U9W}.
STRAND 34 45 {ECO:0000244|PDB:3U9W}.
STRAND 50 59 {ECO:0000244|PDB:3U9W}.
STRAND 61 67 {ECO:0000244|PDB:3U9W}.
STRAND 74 76 {ECO:0000244|PDB:3U9W}.
HELIX 81 83 {ECO:0000244|PDB:3U9W}.
STRAND 85 95 {ECO:0000244|PDB:3U9W}.
STRAND 100 108 {ECO:0000244|PDB:3U9W}.
STRAND 116 119 {ECO:0000244|PDB:3U9W}.
HELIX 121 123 {ECO:0000244|PDB:3U9W}.
STRAND 124 129 {ECO:0000244|PDB:3U9W}.
STRAND 131 134 {ECO:0000244|PDB:3U9W}.
TURN 137 140 {ECO:0000244|PDB:3U9W}.
HELIX 141 143 {ECO:0000244|PDB:3U9W}.
STRAND 155 164 {ECO:0000244|PDB:3U9W}.
STRAND 167 180 {ECO:0000244|PDB:3U9W}.
STRAND 182 184 {ECO:0000244|PDB:2VJ8}.
STRAND 187 198 {ECO:0000244|PDB:3U9W}.
HELIX 200 202 {ECO:0000244|PDB:3U9W}.
STRAND 205 209 {ECO:0000244|PDB:3U9W}.
STRAND 211 216 {ECO:0000244|PDB:3U9W}.
STRAND 219 223 {ECO:0000244|PDB:3U9W}.
HELIX 225 227 {ECO:0000244|PDB:3U9W}.
HELIX 228 234 {ECO:0000244|PDB:3U9W}.
TURN 235 237 {ECO:0000244|PDB:3U9W}.
HELIX 238 249 {ECO:0000244|PDB:3U9W}.
STRAND 258 261 {ECO:0000244|PDB:3U9W}.
STRAND 267 271 {ECO:0000244|PDB:3U9W}.
STRAND 276 279 {ECO:0000244|PDB:3U9W}.
HELIX 281 283 {ECO:0000244|PDB:3U9W}.
STRAND 286 288 {ECO:0000244|PDB:3U9W}.
TURN 289 291 {ECO:0000244|PDB:3U9W}.
HELIX 292 299 {ECO:0000244|PDB:3U9W}.
TURN 300 302 {ECO:0000244|PDB:3U9W}.
TURN 304 306 {ECO:0000244|PDB:3U9W}.
STRAND 307 311 {ECO:0000244|PDB:3U9W}.
HELIX 312 314 {ECO:0000244|PDB:3U9W}.
HELIX 315 334 {ECO:0000244|PDB:3U9W}.
HELIX 336 357 {ECO:0000244|PDB:3U9W}.
HELIX 362 364 {ECO:0000244|PDB:3U9W}.
STRAND 365 367 {ECO:0000244|PDB:3U9W}.
HELIX 375 378 {ECO:0000244|PDB:3U9W}.
HELIX 382 398 {ECO:0000244|PDB:3U9W}.
HELIX 401 415 {ECO:0000244|PDB:3U9W}.
STRAND 418 420 {ECO:0000244|PDB:3U9W}.
HELIX 422 432 {ECO:0000244|PDB:3U9W}.
HELIX 434 436 {ECO:0000244|PDB:3U9W}.
HELIX 437 441 {ECO:0000244|PDB:3U9W}.
HELIX 445 450 {ECO:0000244|PDB:3U9W}.
TURN 464 466 {ECO:0000244|PDB:3U9W}.
HELIX 467 478 {ECO:0000244|PDB:3U9W}.
HELIX 481 486 {ECO:0000244|PDB:3U9W}.
HELIX 489 492 {ECO:0000244|PDB:3U9W}.
HELIX 497 508 {ECO:0000244|PDB:3U9W}.
HELIX 515 525 {ECO:0000244|PDB:3U9W}.
HELIX 527 529 {ECO:0000244|PDB:3U9W}.
HELIX 533 545 {ECO:0000244|PDB:3U9W}.
HELIX 551 561 {ECO:0000244|PDB:3U9W}.
HELIX 565 577 {ECO:0000244|PDB:3U9W}.
HELIX 579 592 {ECO:0000244|PDB:3U9W}.
HELIX 593 595 {ECO:0000244|PDB:3U9W}.
HELIX 598 608 {ECO:0000244|PDB:3U9W}.
SEQUENCE 611 AA; 69285 MW; 329BF6D04D4A06E1 CRC64;
MPEIVDTCSL ASPASVCRTK HLHLRCSVDF TRRTLTGTAA LTVQSQEDNL RSLVLDTKDL
TIEKVVINGQ EVKYALGERQ SYKGSPMEIS LPIALSKNQE IVIEISFETS PKSSALQWLT
PEQTSGKEHP YLFSQCQAIH CRAILPCQDT PSVKLTYTAE VSVPKELVAL MSAIRDGETP
DPEDPSRKIY KFIQKVPIPC YLIALVVGAL ESRQIGPRTL VWSEKEQVEK SAYEFSETES
MLKIAEDLGG PYVWGQYDLL VLPPSFPYGG MENPCLTFVT PTLLAGDKSL SNVIAHEISH
SWTGNLVTNK TWDHFWLNEG HTVYLERHIC GRLFGEKFRH FNALGGWGEL QNSVKTFGET
HPFTKLVVDL TDIDPDVAYS SVPYEKGFAL LFYLEQLLGG PEIFLGFLKA YVEKFSYKSI
TTDDWKDFLY SYFKDKVDVL NQVDWNAWLY SPGLPPIKPN YDMTLTNACI ALSQRWITAK
EDDLNSFNAT DLKDLSSHQL NEFLAQTLQR APLPLGHIKR MQEVYNFNAI NNSEIRFRWL
RLCIQSKWED AIPLALKMAT EQGRMKFTRP LFKDLAAFDK SHDQAVRTYQ EHKASMHPVT
AMLVGKDLKV D


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