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Database: UniProt
Entry: P09960
LinkDB: P09960
Original site: P09960 
ID   LKHA4_HUMAN             Reviewed;         611 AA.
AC   P09960; B4DNQ9; F8VV40; Q6IAT6; Q9UCT7;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   09-JUL-2014, entry version 178.
DE   RecName: Full=Leukotriene A-4 hydrolase;
DE            Short=LTA-4 hydrolase;
DE            EC=3.3.2.6;
DE   AltName: Full=Leukotriene A(4) hydrolase;
GN   Name=LTA4H; Synonyms=LTA4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=3654641;
RA   Minami M., Ohno S., Kawasaki H., Raedmark O., Samuelsson B.,
RA   Joernvall H., Shimizu T., Seyama Y., Suzuki K.;
RT   "Molecular cloning of a cDNA coding for human leukotriene A4
RT   hydrolase. Complete primary structure of an enzyme involved in
RT   eicosanoid synthesis.";
RL   J. Biol. Chem. 262:13873-13876(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2821541; DOI=10.1073/pnas.84.19.6677;
RA   Funk C.D., Raadmark O., Fu J.Y., Matsumoto T., Joernvall H.,
RA   Shimizu T., Samuelsson B.;
RT   "Molecular cloning and amino acid sequence of leukotriene A4
RT   hydrolase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:6677-6681(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7628486; DOI=10.1111/j.1432-1033.1995.tb20671.x;
RA   Mancini J.A., Evans J.F.;
RT   "Cloning and characterization of the human leukotriene A4 hydrolase
RT   gene.";
RL   Eur. J. Biochem. 231:65-71(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Lung;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Esophageal carcinoma;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   PROTEIN SEQUENCE OF 2-22, FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=B-cell;
RX   PubMed=1897988; DOI=10.1016/0003-9861(91)90402-5;
RA   Odlander B., Claesson H.E., Bergman T., Radmark O., Joernvall H.,
RA   Haeggstrom J.Z.;
RT   "Leukotriene A4 hydrolase in the human B-lymphocytic cell line Raji:
RT   indications of catalytically divergent forms of the enzyme.";
RL   Arch. Biochem. Biophys. 287:167-174(1991).
RN   [11]
RP   PROTEIN SEQUENCE OF 2-16.
RX   PubMed=6490615;
RA   Radmark O., Shimizu T., Joernvall H., Samuelsson B.;
RT   "Leukotriene A4 hydrolase in human leukocytes. Purification and
RT   properties.";
RL   J. Biol. Chem. 259:12339-12345(1984).
RN   [12]
RP   PROTEIN SEQUENCE OF 366-386, ENZYME REGULATION, COVALENT MODIFICATION
RP   AT TYR-379, AND CATALYTIC ACTIVITY.
RX   PubMed=7667299; DOI=10.1073/pnas.92.18.8383;
RA   Mueller M.J., Wetterholm A., Blomster M., Jornvall H., Samuelsson B.,
RA   Haeggstrom J.Z.;
RT   "Leukotriene A4 hydrolase: mapping of a henicosapeptide involved in
RT   mechanism-based inactivation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:8383-8387(1995).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 511-611, AND ALTERNATIVE SPLICING
RP   (ISOFORMS 1 AND 2).
RX   PubMed=8615763;
RA   Jendraschak E., Kaminski W.E., Kiefl R., von Schacky C.;
RT   "The human leukotriene A4 hydrolase gene is expressed in two
RT   alternatively spliced mRNA forms.";
RL   Biochem. J. 314:733-737(1996).
RN   [14]
RP   ZINC-BINDING, FUNCTION AS A PEPTIDASE, AND SIMILARITY TO ZINC
RP   PROTEASES.
RX   PubMed=1975494; DOI=10.1016/0006-291X(90)91379-7;
RA   Toh H., Minami M., Shimizu T.;
RT   "Molecular evolution and zinc ion binding motif of leukotriene A4
RT   hydrolase.";
RL   Biochem. Biophys. Res. Commun. 171:216-221(1990).
RN   [15]
RP   ZINC-BINDING, AND FUNCTION AS A PEPTIDASE.
RX   PubMed=2244921; DOI=10.1016/0006-291X(90)91540-9;
RA   Haeggstroem J.Z., Wetterholm A., Shapiro R., Vallee B.L.,
RA   Samuelsson B.;
RT   "Leukotriene A4 hydrolase: a zinc metalloenzyme.";
RL   Biochem. Biophys. Res. Commun. 172:965-970(1990).
RN   [16]
RP   MUTAGENESIS OF ZINC LIGANDS.
RX   PubMed=1881903; DOI=10.1073/pnas.88.17.7620;
RA   Medina J.F., Wetterholm A., Raadmark O., Shapiro R., Haeggstroem J.Z.,
RA   Vallee B.L., Samuelsson B.;
RT   "Leukotriene A4 hydrolase: determination of the three zinc-binding
RT   ligands by site-directed mutagenesis and zinc analysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:7620-7624(1991).
RN   [17]
RP   MUTAGENESIS OF GLU-297.
RX   PubMed=1516710; DOI=10.1016/0014-5793(92)80806-R;
RA   Minami M., Bito H., Ohishi N., Tsuge H., Miyano M., Mori M., Wada H.,
RA   Mutoh H., Shimada S., Izumi T., Abe K., Shimuzu T.;
RT   "Leukotriene A4 hydrolase, a bifunctional enzyme. Distinction of
RT   leukotriene A4 hydrolase and aminopeptidase activities by site-
RT   directed mutagenesis at Glu-297.";
RL   FEBS Lett. 309:353-357(1992).
RN   [18]
RP   MUTAGENESIS OF GLU-297.
RX   PubMed=1357660; DOI=10.1073/pnas.89.19.9141;
RA   Wetterholm A., Medina J.F., Raadmark O., Shapiro R., Haeggstroem J.Z.,
RA   Vallee B.L., Samuelsson B.;
RT   "Leukotriene A4 hydrolase: abrogation of the peptidase activity by
RT   mutation of glutamic acid-296.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:9141-9145(1992).
RN   [19]
RP   PHOSPHORYLATION AT SER-416.
RX   PubMed=9395533; DOI=10.1074/jbc.272.50.31865;
RA   Rybina I.V., Liu H., Gor Y., Feinmark S.J.;
RT   "Regulation of leukotriene A4 hydrolase activity in endothelial cells
RT   by phosphorylation.";
RL   J. Biol. Chem. 272:31865-31871(1997).
RN   [20]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-337; LYS-414 AND
RP   LYS-573, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX   PubMed=11175901; DOI=10.1038/84117;
RA   Thunnissen M.M.G.M., Nordlund P., Haeggstroem J.Z.;
RT   "Crystal structure of human leukotriene A(4) hydrolase, a bifunctional
RT   enzyme in inflammation.";
RL   Nat. Struct. Biol. 8:131-135(2001).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH CAPTOPRIL AND
RP   ZINC IONS, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX   PubMed=12207002; DOI=10.1096/fj.01-1017fje;
RA   Thunnissen M.M., Andersson B., Samuelsson B., Wong C.H.,
RA   Haeggstrom J.Z.;
RT   "Crystal structures of leukotriene A4 hydrolase in complex with
RT   captopril and two competitive tight-binding inhibitors.";
RL   FASEB J. 16:1648-1650(2002).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT GLN-272, AND
RP   MUTAGENESIS OF GLN-137; GLY-270; MET-271; GLU-272 AND ASN-273.
RX   PubMed=11675384; DOI=10.1074/jbc.M106577200;
RA   Rudberg P.C., Tholander F., Thunnissen M.M.G.M., Haeggstroem J.Z.;
RT   "Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic
RT   residue with specific roles in two distinct enzyme mechanisms.";
RL   J. Biol. Chem. 277:1398-1404(2002).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT ASN-376 IN COMPLEX
RP   WITH BESTATIN AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, AND
RP   MUTAGENESIS OF GLN-135; HIS-140; ASP-372; ASP-374; ASP-376 AND
RP   GLU-385.
RX   PubMed=11917124; DOI=10.1073/pnas.072090099;
RA   Rudberg P.C., Tholander F., Thunnissen M.M., Samuelsson B.,
RA   Haeggstrom J.Z.;
RT   "Leukotriene A4 hydrolase: selective abrogation of leukotriene B4
RT   formation by mutation of aspartic acid 375.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4215-4220(2002).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ALA-564 IN COMPLEX
RP   WITH ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, AND
RP   MUTAGENESIS OF ARG-564 AND LYS-566.
RX   PubMed=15078870; DOI=10.1074/jbc.M401031200;
RA   Rudberg P.C., Tholander F., Andberg M., Thunnissen M.M.,
RA   Haeggstrom J.Z.;
RT   "Leukotriene A4 hydrolase: identification of a common carboxylate
RT   recognition site for the epoxide hydrolase and aminopeptidase
RT   substrates.";
RL   J. Biol. Chem. 279:27376-27382(2004).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF MUTANT GLN-297 IN COMPLEXES
RP   WITH SUBSTRATE TRIPEPTIDES AND ZINC IONS, CATALYTIC ACTIVITY,
RP   FUNCTION, COFACTOR, AND MUTAGENESIS OF GLU-297 AND ASP-376.
RX   PubMed=18804029; DOI=10.1016/j.chembiol.2008.07.018;
RA   Tholander F., Muroya A., Roques B.P., Fournie-Zaluski M.C.,
RA   Thunnissen M.M., Haeggstrom J.Z.;
RT   "Structure-based dissection of the active site chemistry of
RT   leukotriene A4 hydrolase: implications for M1 aminopeptidases and
RT   inhibitor design.";
RL   Chem. Biol. 15:920-929(2008).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) IN COMPLEXES WITH INHIBITORS
RP   AND ZINC IONS.
RX   PubMed=19618939; DOI=10.1021/jm900259h;
RA   Davies D.R., Mamat B., Magnusson O.T., Christensen J.,
RA   Haraldsson M.H., Mishra R., Pease B., Hansen E., Singh J.,
RA   Zembower D., Kim H., Kiselyov A.S., Burgin A.B., Gurney M.E.,
RA   Stewart L.J.;
RT   "Discovery of leukotriene A4 hydrolase inhibitors using metabolomics
RT   biased fragment crystallography.";
RL   J. Med. Chem. 52:4694-4715(2009).
CC   -!- FUNCTION: Epoxide hydrolase that catalyzes the final step in the
CC       biosynthesis of the proinflammatory mediator leukotriene B4. Has
CC       also aminopeptidase activity.
CC   -!- CATALYTIC ACTIVITY: (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-
CC       7,9,11,14-tetraenoate + H(2)O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-
CC       dihydroxyicosa-6,8,10,14-tetraenoate.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit.
CC   -!- ENZYME REGULATION: Inhibited by bestatin. Subject to suicide
CC       inhibition by leukotriene A4, due to the formation of a covalent
CC       adduct at Tyr-379.
CC   -!- PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=L-LTA4;
CC         IsoId=P09960-1; Sequence=Displayed;
CC       Name=2; Synonyms=S-LTA4;
CC         IsoId=P09960-2; Sequence=VSP_041108, VSP_041109;
CC       Name=3;
CC         IsoId=P09960-3; Sequence=VSP_041107, VSP_041108, VSP_041109;
CC       Name=4;
CC         IsoId=P09960-4; Sequence=VSP_041107;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in
CC       monocytes, lymphocytes, neutrophils, reticulocytes, platelets and
CC       fibroblasts.
CC   -!- PTM: Phosphorylation at Ser-416 inhibits enzymatic activity.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
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DR   EMBL; J03459; AAA36176.1; -; mRNA.
DR   EMBL; J02959; AAA36177.1; -; mRNA.
DR   EMBL; U27293; AAA89077.1; -; Genomic_DNA.
DR   EMBL; U27275; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27276; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27277; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27278; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27279; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27280; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27281; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27282; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27283; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27284; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27285; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27286; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27287; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27288; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27289; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27290; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27291; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27292; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; AK298017; BAG60321.1; -; mRNA.
DR   EMBL; CR457068; CAG33349.1; -; mRNA.
DR   EMBL; BX647158; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC007298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471054; EAW97559.1; -; Genomic_DNA.
DR   EMBL; BC032528; AAH32528.1; -; mRNA.
DR   EMBL; U43410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U43411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS58266.1; -. [P09960-3]
DR   CCDS; CCDS58267.1; -. [P09960-4]
DR   CCDS; CCDS9059.1; -. [P09960-1]
DR   PIR; S65947; S65947.
DR   RefSeq; NP_000886.1; NM_000895.2. [P09960-1]
DR   RefSeq; NP_001243572.1; NM_001256643.1. [P09960-4]
DR   RefSeq; NP_001243573.1; NM_001256644.1. [P09960-3]
DR   RefSeq; XP_005268928.1; XM_005268871.1. [P09960-2]
DR   UniGene; Hs.524648; -.
DR   PDB; 1GW6; X-ray; 2.20 A; A=2-611.
DR   PDB; 1H19; X-ray; 2.10 A; A=2-611.
DR   PDB; 1HS6; X-ray; 1.95 A; A=1-611.
DR   PDB; 1SQM; X-ray; 2.30 A; A=2-611.
DR   PDB; 2R59; X-ray; 1.89 A; A=2-611.
DR   PDB; 2VJ8; X-ray; 1.80 A; A=1-611.
DR   PDB; 3B7R; X-ray; 1.81 A; L=2-611.
DR   PDB; 3B7S; X-ray; 1.47 A; A=2-611.
DR   PDB; 3B7T; X-ray; 2.30 A; A=2-611.
DR   PDB; 3B7U; X-ray; 1.90 A; X=2-611.
DR   PDB; 3CHO; X-ray; 1.80 A; A=2-611.
DR   PDB; 3CHP; X-ray; 2.10 A; A=2-611.
DR   PDB; 3CHQ; X-ray; 2.09 A; A=2-611.
DR   PDB; 3CHR; X-ray; 2.20 A; A=2-611.
DR   PDB; 3CHS; X-ray; 2.55 A; A=2-611.
DR   PDB; 3FH5; X-ray; 1.63 A; A=1-611.
DR   PDB; 3FH7; X-ray; 2.05 A; A=1-611.
DR   PDB; 3FH8; X-ray; 1.67 A; A=1-611.
DR   PDB; 3FHE; X-ray; 2.16 A; A=1-611.
DR   PDB; 3FTS; X-ray; 2.33 A; A=1-611.
DR   PDB; 3FTU; X-ray; 1.90 A; A=1-611.
DR   PDB; 3FTV; X-ray; 1.70 A; A=1-611.
DR   PDB; 3FTW; X-ray; 1.85 A; A=1-611.
DR   PDB; 3FTX; X-ray; 1.96 A; A=1-611.
DR   PDB; 3FTY; X-ray; 2.15 A; A=1-611.
DR   PDB; 3FTZ; X-ray; 2.00 A; A=1-611.
DR   PDB; 3FU0; X-ray; 1.80 A; A=1-611.
DR   PDB; 3FU3; X-ray; 2.00 A; A=1-611.
DR   PDB; 3FU5; X-ray; 2.30 A; A=1-611.
DR   PDB; 3FU6; X-ray; 2.05 A; A=1-611.
DR   PDB; 3FUD; X-ray; 2.20 A; A=1-611.
DR   PDB; 3FUE; X-ray; 2.38 A; A=1-611.
DR   PDB; 3FUF; X-ray; 2.60 A; A=1-611.
DR   PDB; 3FUH; X-ray; 1.80 A; A=1-611.
DR   PDB; 3FUI; X-ray; 2.20 A; A=1-611.
DR   PDB; 3FUJ; X-ray; 1.90 A; A=1-611.
DR   PDB; 3FUK; X-ray; 1.95 A; A=1-611.
DR   PDB; 3FUL; X-ray; 2.39 A; A=1-611.
DR   PDB; 3FUM; X-ray; 2.15 A; A=1-611.
DR   PDB; 3FUN; X-ray; 1.58 A; A=1-611.
DR   PDB; 3U9W; X-ray; 1.25 A; A=4-611.
DR   PDB; 4DPR; X-ray; 2.02 A; A=1-611.
DR   PDB; 4L2L; X-ray; 1.65 A; A=1-611.
DR   PDB; 4MKT; X-ray; 1.62 A; A=1-611.
DR   PDB; 4MS6; X-ray; 1.72 A; A=1-611.
DR   PDBsum; 1GW6; -.
DR   PDBsum; 1H19; -.
DR   PDBsum; 1HS6; -.
DR   PDBsum; 1SQM; -.
DR   PDBsum; 2R59; -.
DR   PDBsum; 2VJ8; -.
DR   PDBsum; 3B7R; -.
DR   PDBsum; 3B7S; -.
DR   PDBsum; 3B7T; -.
DR   PDBsum; 3B7U; -.
DR   PDBsum; 3CHO; -.
DR   PDBsum; 3CHP; -.
DR   PDBsum; 3CHQ; -.
DR   PDBsum; 3CHR; -.
DR   PDBsum; 3CHS; -.
DR   PDBsum; 3FH5; -.
DR   PDBsum; 3FH7; -.
DR   PDBsum; 3FH8; -.
DR   PDBsum; 3FHE; -.
DR   PDBsum; 3FTS; -.
DR   PDBsum; 3FTU; -.
DR   PDBsum; 3FTV; -.
DR   PDBsum; 3FTW; -.
DR   PDBsum; 3FTX; -.
DR   PDBsum; 3FTY; -.
DR   PDBsum; 3FTZ; -.
DR   PDBsum; 3FU0; -.
DR   PDBsum; 3FU3; -.
DR   PDBsum; 3FU5; -.
DR   PDBsum; 3FU6; -.
DR   PDBsum; 3FUD; -.
DR   PDBsum; 3FUE; -.
DR   PDBsum; 3FUF; -.
DR   PDBsum; 3FUH; -.
DR   PDBsum; 3FUI; -.
DR   PDBsum; 3FUJ; -.
DR   PDBsum; 3FUK; -.
DR   PDBsum; 3FUL; -.
DR   PDBsum; 3FUM; -.
DR   PDBsum; 3FUN; -.
DR   PDBsum; 3U9W; -.
DR   PDBsum; 4DPR; -.
DR   PDBsum; 4L2L; -.
DR   PDBsum; 4MKT; -.
DR   PDBsum; 4MS6; -.
DR   ProteinModelPortal; P09960; -.
DR   SMR; P09960; 4-611.
DR   BioGrid; 110226; 12.
DR   IntAct; P09960; 5.
DR   MINT; MINT-1388946; -.
DR   STRING; 9606.ENSP00000228740; -.
DR   BindingDB; P09960; -.
DR   ChEMBL; CHEMBL4618; -.
DR   GuidetoPHARMACOLOGY; 1395; -.
DR   MEROPS; M01.004; -.
DR   PhosphoSite; P09960; -.
DR   DMDM; 126353; -.
DR   REPRODUCTION-2DPAGE; IPI00219077; -.
DR   MaxQB; P09960; -.
DR   PaxDb; P09960; -.
DR   PRIDE; P09960; -.
DR   DNASU; 4048; -.
DR   Ensembl; ENST00000228740; ENSP00000228740; ENSG00000111144. [P09960-1]
DR   Ensembl; ENST00000413268; ENSP00000395051; ENSG00000111144. [P09960-3]
DR   Ensembl; ENST00000552789; ENSP00000449958; ENSG00000111144. [P09960-4]
DR   GeneID; 4048; -.
DR   KEGG; hsa:4048; -.
DR   UCSC; uc001ten.2; human. [P09960-1]
DR   UCSC; uc010suz.2; human. [P09960-3]
DR   CTD; 4048; -.
DR   GeneCards; GC12M096394; -.
DR   HGNC; HGNC:6710; LTA4H.
DR   HPA; CAB015221; -.
DR   HPA; HPA008399; -.
DR   HPA; HPA017017; -.
DR   MIM; 151570; gene.
DR   neXtProt; NX_P09960; -.
DR   PharmGKB; PA24345; -.
DR   eggNOG; COG0308; -.
DR   HOGENOM; HOG000293296; -.
DR   HOVERGEN; HBG001274; -.
DR   InParanoid; P09960; -.
DR   KO; K01254; -.
DR   OMA; SPASVCQ; -.
DR   OrthoDB; EOG7SJD42; -.
DR   PhylomeDB; P09960; -.
DR   TreeFam; TF300758; -.
DR   BioCyc; MetaCyc:HS03372-MONOMER; -.
DR   BRENDA; 3.3.2.6; 2681.
DR   Reactome; REACT_111217; Metabolism.
DR   UniPathway; UPA00878; -.
DR   ChiTaRS; LTA4H; human.
DR   EvolutionaryTrace; P09960; -.
DR   GenomeRNAi; 4048; -.
DR   NextBio; 15856; -.
DR   PRO; PR:P09960; -.
DR   ArrayExpress; P09960; -.
DR   Bgee; P09960; -.
DR   CleanEx; HS_LTA4H; -.
DR   Genevestigator; P09960; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0004301; F:epoxide hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0004463; F:leukotriene-A4 hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; TAS:ProtInc.
DR   GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; TAS:Reactome.
DR   GO; GO:0006954; P:inflammatory response; NAS:ProtInc.
DR   GO; GO:0019370; P:leukotriene biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0006691; P:leukotriene metabolic process; TAS:Reactome.
DR   GO; GO:0043171; P:peptide catabolic process; IDA:UniProtKB.
DR   GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR012777; Leukotriene_A4_hydrolase.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR015211; Peptidase_M1_C.
DR   InterPro; IPR014782; Peptidase_M1_N.
DR   PANTHER; PTHR11533; PTHR11533; 1.
DR   Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   TIGRFAMs; TIGR02411; leuko_A4_hydro; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW   Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Leukotriene biosynthesis; Metal-binding; Metalloprotease;
KW   Phosphoprotein; Polymorphism; Protease; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    611       Leukotriene A-4 hydrolase.
FT                                /FTId=PRO_0000095124.
FT   REGION      135    137       Substrate binding.
FT   REGION      267    272       Substrate binding.
FT   REGION      564    566       Substrate binding.
FT   ACT_SITE    297    297       Proton acceptor (Probable).
FT   ACT_SITE    384    384       Proton donor (Probable).
FT   METAL       296    296       Zinc; catalytic.
FT   METAL       300    300       Zinc; catalytic.
FT   METAL       319    319       Zinc; catalytic.
FT   SITE        376    376       Essential for epoxide hydrolase activity,
FT                                but not for aminopeptidase activity.
FT   SITE        379    379       Covalently modified during suicide
FT                                inhibition by leukotrienes.
FT   MOD_RES      73     73       N6-acetyllysine.
FT   MOD_RES     337    337       N6-acetyllysine.
FT   MOD_RES     414    414       N6-acetyllysine.
FT   MOD_RES     416    416       Phosphoserine.
FT   MOD_RES     573    573       N6-acetyllysine.
FT   VAR_SEQ       1     53       MPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAAL
FT                                TVQSQEDNLRSL -> MLPQRNLSKRQVPTMHIPVKTRRLL
FT                                AALK (in isoform 3 and isoform 4).
FT                                /FTId=VSP_041107.
FT   VAR_SEQ     511    532       APLPLGHIKRMQEVYNFNAINN -> MAAALHSIQVGGRNS
FT                                FGAKDGN (in isoform 2 and isoform 3).
FT                                /FTId=VSP_041108.
FT   VAR_SEQ     533    611       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_041109.
FT   VARIANT     131    131       Y -> H (in dbSNP:rs45630737).
FT                                /FTId=VAR_051570.
FT   MUTAGEN     135    135       Q->A,L: Srongly increased epoxide
FT                                hydrolase activity.
FT   MUTAGEN     135    135       Q->A: Strongly reduced aminopeptidase
FT                                activity. Strongly decreased affinity for
FT                                leukotriene. Abolishes epoxide hydrolase
FT                                activity.
FT   MUTAGEN     137    137       Q->A: No loss of activity.
FT   MUTAGEN     137    137       Q->L: Aminopeptidase activity strongly
FT                                impaired, but keeps LTA4 activity.
FT   MUTAGEN     137    137       Q->N: Aminopeptidase activity almost
FT                                absent, but keeps LTA4 activity.
FT   MUTAGEN     140    140       H->Q: Aminopeptidase activity almost
FT                                absent, but keeps LTA4 activity.
FT   MUTAGEN     269    269       G->A: No loss of activity.
FT   MUTAGEN     270    270       G->A: No loss of activity.
FT   MUTAGEN     271    271       M->L: No loss of activity.
FT   MUTAGEN     272    272       E->A,D: Complete loss of activity.
FT   MUTAGEN     272    272       E->Q: Loss of LTA4 activity, and
FT                                aminopeptidase activity strongly
FT                                impaired.
FT   MUTAGEN     273    273       N->A: No loss of activity.
FT   MUTAGEN     296    296       H->Y: Complete loss of activity.
FT   MUTAGEN     297    297       E->A: Loss of both activities.
FT   MUTAGEN     297    297       E->K: Loss of both activities.
FT   MUTAGEN     297    297       E->Q: Loss of aminopeptidase activity,
FT                                but keeps LTA4 activity.
FT   MUTAGEN     300    300       H->L: Complete loss of activity.
FT   MUTAGEN     319    319       E->A: Complete loss of activity.
FT   MUTAGEN     372    372       D->N: No loss of activity.
FT   MUTAGEN     374    374       D->N: No loss of activity.
FT   MUTAGEN     376    376       D->A: Strongly reduced hydrolysis of
FT                                peptides starting with Arg. Small effect
FT                                on hydrolysis of peptides starting with
FT                                Ala. Strongly reduced epoxide hydrolase
FT                                activity.
FT   MUTAGEN     376    376       D->E: Strongly reduced aminopeptidase
FT                                activity. Abolishes epoxide hydrolase
FT                                activity.
FT   MUTAGEN     376    376       D->N: Abolishes aminopeptidase and
FT                                epoxide hydrolase activity.
FT   MUTAGEN     385    385       E->Q: Reduced aminopeptidase activity.
FT                                Minor effect on epoxide hydrolase
FT                                activity.
FT   MUTAGEN     564    564       R->A,K,M: Abolishes epoxide hydrolase
FT                                activity. Reduced aminopeptidase
FT                                activity.
FT   MUTAGEN     566    566       K->A,M: Strongly reduced affinity for
FT                                peptide substrates. Reduced epoxide
FT                                hydrolase and aminopeptidase activity.
FT   MUTAGEN     566    566       K->R: No effect on epoxide hydrolase and
FT                                aminopeptidase activity.
FT   CONFLICT    115    115       A -> T (in Ref. 6; BX647158).
FT   CONFLICT    123    123       Q -> R (in Ref. 6; BX647158).
FT   CONFLICT    297    297       E -> G (in Ref. 4; BAG60321).
FT   CONFLICT    309    309       N -> S (in Ref. 6; BX647158).
FT   CONFLICT    378    378       A -> V (in Ref. 6; BX647158).
FT   TURN         14     16
FT   STRAND       17     29
FT   TURN         30     33
FT   STRAND       34     45
FT   STRAND       50     59
FT   STRAND       61     67
FT   STRAND       74     76
FT   HELIX        81     83
FT   STRAND       85     95
FT   STRAND      100    108
FT   STRAND      116    119
FT   HELIX       121    123
FT   STRAND      124    129
FT   STRAND      131    134
FT   TURN        137    140
FT   HELIX       141    143
FT   STRAND      155    164
FT   STRAND      167    180
FT   STRAND      182    184
FT   STRAND      187    198
FT   HELIX       200    202
FT   STRAND      205    209
FT   STRAND      211    216
FT   STRAND      219    223
FT   HELIX       225    227
FT   HELIX       228    234
FT   TURN        235    237
FT   HELIX       238    249
FT   STRAND      258    261
FT   STRAND      267    271
FT   STRAND      276    279
FT   HELIX       281    283
FT   STRAND      286    288
FT   TURN        289    291
FT   HELIX       292    299
FT   TURN        300    302
FT   TURN        304    306
FT   STRAND      307    311
FT   HELIX       312    314
FT   HELIX       315    334
FT   HELIX       336    357
FT   HELIX       362    364
FT   STRAND      365    367
FT   HELIX       375    378
FT   HELIX       382    398
FT   HELIX       401    415
FT   STRAND      418    420
FT   HELIX       422    432
FT   HELIX       434    436
FT   HELIX       437    441
FT   HELIX       445    450
FT   TURN        464    466
FT   HELIX       467    478
FT   HELIX       481    486
FT   HELIX       489    492
FT   HELIX       497    508
FT   HELIX       515    525
FT   HELIX       527    529
FT   HELIX       533    545
FT   HELIX       551    561
FT   HELIX       565    577
FT   HELIX       579    592
FT   HELIX       593    595
FT   HELIX       598    608
SQ   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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