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Volumn 4, Issue 12, 1997, Pages 1003-1009

The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity

Author keywords

[No Author keywords available]

Indexed keywords

ARACHIDONATE 15 LIPOXYGENASE; TRIACYLGLYCEROL LIPASE;

EID: 0030736867     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb1297-1003     Document Type: Article
Times cited : (403)

References (43)
  • 1
    • 0023177955 scopus 로고
    • Leukotrienes and Lipoxins: Structures, Biosynthesis, and Biological Effects
    • Samuelsson, B., Dahlén, S.-E., Lingren, J.Å., Rouzer, C.A. & Serhan, C.N. Leukotrienes and Lipoxins: Structures, Biosynthesis, and Biological Effects, Science 237, 1171-1176 (1987).
    • (1987) Science , vol.237 , pp. 1171-1176
    • Samuelsson, B.1    Dahlén, S.-E.2    Lingren, J.Å.3    Rouzer, C.A.4    Serhan, C.N.5
  • 2
    • 0030976460 scopus 로고    scopus 로고
    • A G-protein coupled receptor for leukotriene B4 that mediates chemotaxis
    • Yokomizo, T., Izumi, T., Chang, K., Takuwa, Y. & Shimizu, T. A G-protein coupled receptor for leukotriene B4 that mediates chemotaxis. Nature 387, 620-624 (1997).
    • (1997) Nature , vol.387 , pp. 620-624
    • Yokomizo, T.1    Izumi, T.2    Chang, K.3    Takuwa, Y.4    Shimizu, T.5
  • 3
    • 0029661982 scopus 로고    scopus 로고
    • The PPARa-Leukotriene B4 pathway to inflammation control
    • Devchand, P.R. et al. The PPARa-Leukotriene B4 pathway to inflammation control. Nature 384, 39-43 (1996).
    • (1996) Nature , vol.384 , pp. 39-43
    • Devchand, P.R.1
  • 4
    • 0030952937 scopus 로고    scopus 로고
    • Hypolipidemic drugs, polyunsaturated fatty acids, and eicosanoids are ligands for peroxisome proliferator-activated receptors alpha and delta
    • Forman, B.M., Chen, J. & Evans, R.M. Hypolipidemic drugs, polyunsaturated fatty acids, and eicosanoids are ligands for peroxisome proliferator-activated receptors alpha and delta. Proc Nat. Acad Sci. USA 94, 4312-4317 (1997).
    • (1997) Proc Nat. Acad Sci. USA , vol.94 , pp. 4312-4317
    • Forman, B.M.1    Chen, J.2    Evans, R.M.3
  • 5
    • 0029915834 scopus 로고    scopus 로고
    • Effect of treatment with Zileuton, a 5-lipoxygenase inhibitor, in patients with asthma
    • Israel, E., Cohn, J., Dubé, L. & Drazen, J.M. Effect of treatment with Zileuton, a 5-lipoxygenase inhibitor, in patients with asthma. J. Am. Med Assn. 275, 931-936 (1996).
    • (1996) J. Am. Med Assn. , vol.275 , pp. 931-936
    • Israel, E.1    Cohn, J.2    Dubé, L.3    Drazen, J.M.4
  • 6
    • 0027393863 scopus 로고
    • Induction of epithelial arachidonate 12-lipoxygenase at active sites of inflammatory bowel disease
    • Shannon, V.R., Stenson, W.F. & Holtzman, M.J. Induction of epithelial arachidonate 12-lipoxygenase at active sites of inflammatory bowel disease. Am. J. Physiol. 264, G104-111 (1993).
    • (1993) Am. J. Physiol. , vol.264
    • Shannon, V.R.1    Stenson, W.F.2    Holtzman, M.J.3
  • 7
    • 0024603895 scopus 로고
    • Beyond cholesterol: Modifications of low-density lipoprotein that increase its atherogenicity
    • Steinberg, D., Parthasarathy, S., Carew, T.E., Khoo, J.C. & Witztum, M.D. Beyond cholesterol: Modifications of low-density lipoprotein that increase its atherogenicity. N. Engl. J. Med. 320, 915-924(1989).
    • (1989) N. Engl. J. Med. , vol.320 , pp. 915-924
    • Steinberg, D.1    Parthasarathy, S.2    Carew, T.E.3    Khoo, J.C.4    Witztum, M.D.5
  • 8
    • 0025897282 scopus 로고
    • Gene expression in macrophage-rich human atherosclerotic lesions, 15-lipoxygenase and acetyl low density lipoprotein receptor messenger RNA colocalize with oxidation specific lipid-protein adducts
    • Yla-Herttuala, S. et al. Gene expression in macrophage-rich human atherosclerotic lesions, 15-lipoxygenase and acetyl low density lipoprotein receptor messenger RNA colocalize with oxidation specific lipid-protein adducts. J. Clin. Invest 87, 1146-1152 (1991).
    • (1991) J. Clin. Invest , vol.87 , pp. 1146-1152
    • Yla-Herttuala, S.1
  • 9
    • 0028234336 scopus 로고
    • Involvement of 15-lipoxygenase in early stages of atherosclerosis
    • Kühn, J., Belkner, J., Zaiss, S., Fahrenklemper, T. & Wohlfeil, S. Involvement of 15-lipoxygenase in early stages of atherosclerosis. J. Exp. Med. 179, 1903-1911 (1994).
    • (1994) J. Exp. Med. , vol.179 , pp. 1903-1911
    • Kühn, J.1    Belkner, J.2    Zaiss, S.3    Fahrenklemper, T.4    Wohlfeil, S.5
  • 10
    • 0025864367 scopus 로고
    • Arachidonate 15-lipoxygenase; characteristics and potential biological significance
    • Ford-Hutchinson, A.W. Arachidonate 15-lipoxygenase; characteristics and potential biological significance. Eicosanoids 4, 65-74 (1991).
    • (1991) Eicosanoids , vol.4 , pp. 65-74
    • Ford-Hutchinson, A.W.1
  • 11
    • 0028103275 scopus 로고
    • The CCP4 Suite:Programs for protein crystallography
    • The CCP4 Suite:Programs for protein crystallography. Acta Crystallogr. D50, 760-763 (1994).
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 12
    • 0029740369 scopus 로고    scopus 로고
    • Crystal structure of soybean lipoxygenase-1 at 1.4Å resolution
    • Minor, W. et al. Crystal structure of soybean lipoxygenase-1 at 1.4Å resolution. Biochemistry 35, 10687-10701 (1996).
    • (1996) Biochemistry , vol.35 , pp. 10687-10701
    • Minor, W.1
  • 13
    • 0027246677 scopus 로고
    • The three-dimensional structure of an arachidonic acid 15-lipoxygenase
    • Boyington, J.C., Gaffney, B.J. & Amzel, LM. The three-dimensional structure of an arachidonic acid 15-lipoxygenase. Science 260, 1482-1486 (1993).
    • (1993) Science , vol.260 , pp. 1482-1486
    • Boyington, J.C.1    Gaffney, B.J.2    Amzel, L.M.3
  • 14
    • 0030580406 scopus 로고    scopus 로고
    • The molecular biology of mammalian lipoxygenases and the quest for eicosanoid functions using lipoxygenase-deficient mice
    • Funk, C.D. The molecular biology of mammalian lipoxygenases and the quest for eicosanoid functions using lipoxygenase-deficient mice. Biochem. Biophys. Acta 1304, 65-84 (1996).
    • (1996) Biochem. Biophys. Acta , vol.1304 , pp. 65-84
    • Funk, C.D.1
  • 15
    • 0029864977 scopus 로고    scopus 로고
    • Structure conservation in lipoyxgenases: Structural analysis of soybean lipoxygenase-1 and modeling of human lipoxygenases
    • Prigge, S.T., Boyingtoa, J.C., Gaffney, B.J. & Amzel, L.M. Structure conservation in lipoyxgenases: structural analysis of soybean lipoxygenase-1 and modeling of human lipoxygenases. Proteins 24, 275-291 (1996).
    • (1996) Proteins , vol.24 , pp. 275-291
    • Prigge, S.T.1    Boyingtoa, J.C.2    Gaffney, B.J.3    Amzel, L.M.4
  • 16
    • 0024271247 scopus 로고
    • Molecular cloning and primary structure of human 15-lipoxygenase
    • Sigal, E. et al. Molecular cloning and primary structure of human 15-lipoxygenase. Biochem. Biophys. Res, Comm. 157, 457-464 (1988).
    • (1988) Biochem. Biophys. Res, Comm. , vol.157 , pp. 457-464
    • Sigal, E.1
  • 17
    • 0025062291 scopus 로고
    • Structure of human pancreatic lipase
    • Winkler, F.W., D'Arcy, A. & Hunziker, W. Structure of human pancreatic lipase. Nature 343, 771-774 (1990).
    • (1990) Nature , vol.343 , pp. 771-774
    • Winkler, F.W.1    D'Arcy, A.2    Hunziker, W.3
  • 18
    • 0028206237 scopus 로고
    • The carboxyl-terminal domain of lipoprotein lipase binds to the low density lipoprotein receptor related protein/a2-macroglobulin receptor (LRP) and mediates binding of normal very low density lipoproteinsto LRP
    • Williams, S.E. et al. The carboxyl-terminal domain of lipoprotein lipase binds to the low density lipoprotein receptor related protein/a2-macroglobulin receptor (LRP) and mediates binding of normal very low density lipoproteinsto LRP. J. Biol. Chem. 269, 8653-8658 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 8653-8658
    • Williams, S.E.1
  • 19
    • 0026687923 scopus 로고
    • Structure of the pancreatic lipase-procolipase complex
    • Van Tilbeurgh, H., Sarda, L., Verger, R. & Cambillau, C. Structure of the pancreatic lipase-procolipase complex. Nature 359, 159-163 (1992).
    • (1992) Nature , vol.359 , pp. 159-163
    • Van Tilbeurgh, H.1    Sarda, L.2    Verger, R.3    Cambillau, C.4
  • 20
    • 0040544480 scopus 로고    scopus 로고
    • Pancreatic lipase structure-funtion relationships by domain exchange
    • Carriere, F. et al. Pancreatic lipase structure-funtion relationships by domain exchange, Biochemstry 36, 239-248 (1997).
    • (1997) Biochemstry , vol.36 , pp. 239-248
    • Carriere, F.1
  • 21
    • 0025021789 scopus 로고
    • Identification and isolation of a membrane protein necessary for leukotriene production
    • Miller, D.K. et al. Identification and isolation of a membrane protein necessary for leukotriene production. Nature 343, 278-281 (1990).
    • (1990) Nature , vol.343 , pp. 278-281
    • Miller, D.K.1
  • 22
    • 0025022489 scopus 로고
    • Requirement of a 5-lipoxygenase activating protein for leukotriene synthesis
    • Dixon, R.A.F. et al. Requirement of a 5-lipoxygenase activating protein for leukotriene synthesis. Nature 343, 282-284 (1990).
    • (1990) Nature , vol.343 , pp. 282-284
    • Dixon, R.A.F.1
  • 23
    • 0028877549 scopus 로고
    • EPR definition of the non-heme ferric active sites of mammalian 15-lipoxygenase: Major spectral difference relative to human 5-lipoxygenase and plant lipoxygenase and their ligand field origin
    • Zhang, Y., Gan, Q.-F., Ravel, E.G., Sigal, E. & Solomon, E.I. EPR definition of the non-heme ferric active sites of mammalian 15-lipoxygenase: major spectral difference relative to human 5-lipoxygenase and plant lipoxygenase and their ligand field origin. J. Am. Chem. Soc 117, 7422-7427 (1995).
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 7422-7427
    • Zhang, Y.1    Gan, Q.-F.2    Ravel, E.G.3    Sigal, E.4    Solomon, E.I.5
  • 24
    • 0029770071 scopus 로고    scopus 로고
    • (Carboxyalkyl)benzyl propargyl ethers as selective inhibitors of leukocyte-type 12-lipoxygenases
    • Gorins, G., Kuhnert, L., Johnson, CR. & Marnett, L.J. (Carboxyalkyl)benzyl propargyl ethers as selective inhibitors of leukocyte-type 12-lipoxygenases. J. Med. Chem. 39, 4871-4878 (1996).
    • (1996) J. Med. Chem. , vol.39 , pp. 4871-4878
    • Gorins, G.1    Kuhnert, L.2    Johnson, C.R.3    Marnett, L.J.4
  • 25
    • 33845281036 scopus 로고
    • Evidence in favor of an organoiron-mediated pathway for lipoxygenation of fatty acids by soybean lipoxygenase
    • Corey, E.J. & Nagata, R. Evidence in favor of an organoiron-mediated pathway for lipoxygenation of fatty acids by soybean lipoxygenase. J Am. Chem. Soc. 109, 8107-8108 (1987).
    • (1987) J Am. Chem. Soc. , vol.109 , pp. 8107-8108
    • Corey, E.J.1    Nagata, R.2
  • 26
    • 0016426393 scopus 로고
    • Demonstration by EPR spectroscopy of the functional role of iron in soybean lipoxygenase-1
    • de Groot, J.J. et al. Demonstration by EPR spectroscopy of the functional role of iron in soybean lipoxygenase-1. Biochim. Biophys. Acta 377, 71-79 (1975).
    • (1975) Biochim. Biophys. Acta , vol.377 , pp. 71-79
    • De Groot, J.J.1
  • 27
    • 0029843150 scopus 로고    scopus 로고
    • Lipoxygenase reaction mechanism: Demonstration that hydrogen abstraction from substrate predeces dioxygen binding during catalytic turnover
    • Glickman, M.H. & Klinman, J.P. Lipoxygenase reaction mechanism: demonstration that hydrogen abstraction from substrate predeces dioxygen binding during catalytic turnover Biochemistry 35, 12881-12892 (1996).
    • (1996) Biochemistry , vol.35 , pp. 12881-12892
    • Glickman, M.H.1    Klinman, J.P.2
  • 28
    • 0029795583 scopus 로고    scopus 로고
    • Defining the arachidonic acid binding site of human 15-lipoxygenase. Molecular modeling and mutagenesis
    • Gan, Q.F., Browner, M.F., Sloane, D.L & Sigal, E. Defining the arachidonic acid binding site of human 15-lipoxygenase. Molecular modeling and mutagenesis. J. Biol. Chem. 271, 25412-25418 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 25412-25418
    • Gan, Q.F.1    Browner, M.F.2    Sloane, D.L.3    Sigal, E.4
  • 29
    • 0026072935 scopus 로고
    • A primary determinant for lipoxygenase positional specificity
    • Sloane, D.L, Leung, R., Craik, C.S. & Sigal, E. A primary determinant for lipoxygenase positional specificity. Nature 354, 149-152 (1991).
    • (1991) Nature , vol.354 , pp. 149-152
    • Sloane, D.L.1    Leung, R.2    Craik, C.S.3    Sigal, E.4
  • 30
    • 0027166718 scopus 로고
    • Structure-function properties of human platelet 12-lipoxygenase: Chimeric enzyme and in vitro mutagenesis studies
    • Chen, X.S. & Funk, C.D. Structure-function properties of human platelet 12-lipoxygenase: chimeric enzyme and in vitro mutagenesis studies. Faseb J. 7, 694-701 (1993).
    • (1993) Faseb J. , vol.7 , pp. 694-701
    • Chen, X.S.1    Funk, C.D.2
  • 31
    • 0030596087 scopus 로고    scopus 로고
    • Phenylalanine 353 is a primary determinant for the positional specificity of Mammalian 15-lipoxygenases
    • Borngräber, S., Kuban, R.-J., Anton, M. & Kühn, H. Phenylalanine 353 is a primary determinant for the positional specificity of Mammalian 15-lipoxygenases. J. Mol Biol. 264, 1145-1153 (1996).
    • (1996) J. Mol Biol. , vol.264 , pp. 1145-1153
    • Borngräber, S.1    Kuban, R.-J.2    Anton, M.3    Kühn, H.4
  • 33
    • 0022503366 scopus 로고
    • Enzymology and Physiology of reticulocyte lipoxygenase; comparison with other lipoxygenases
    • ed. Meister, A. (John Wiley and Sons, New York)
    • Schewe, T., Rapoport S.M. & Kuhn, H. Enzymology and Physiology of reticulocyte lipoxygenase; comparison with other lipoxygenases. in Advances in enzymology Vol. 58 (ed. Meister, A.) 191-272 (John Wiley and Sons, New York, 1986).
    • (1986) Advances in Enzymology , vol.58 , pp. 191-272
    • Schewe, T.1    Rapoport, S.M.2    Kuhn, H.3
  • 34
    • 0028009093 scopus 로고
    • The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1
    • Picot, D., Loll, P.J. & Garavito, R.M. The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1. Nature 367, 243-249 (1994).
    • (1994) Nature , vol.367 , pp. 243-249
    • Picot, D.1    Loll, P.J.2    Garavito, R.M.3
  • 35
    • 0029911267 scopus 로고    scopus 로고
    • Flexibility of the NSAID binding site in the structure of human cyclooxygenase-2
    • Luong, C. et al. Flexibility of the NSAID binding site in the structure of human cyclooxygenase-2. Nature Struct Biol. 3, 927-933 (1996).
    • (1996) Nature Struct Biol. , vol.3 , pp. 927-933
    • Luong, C.1
  • 36
    • 0031013972 scopus 로고    scopus 로고
    • The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate palmitoleic acid
    • Li, H. & Poulos, T.L. The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate palmitoleic acid. Nature Struct Biol. 4, 140-146 (1997).
    • (1997) Nature Struct Biol. , vol.4 , pp. 140-146
    • Li, H.1    Poulos, T.L.2
  • 37
    • 0025602476 scopus 로고
    • Purification and crystallization of 15-lipoxygenase from rabbit reticulocytes
    • Sloane, D.L. et al. Purification and crystallization of 15-lipoxygenase from rabbit reticulocytes. Biochem. Biophys. Res. Comm. 173, 507-513 (1990).
    • (1990) Biochem. Biophys. Res. Comm. , vol.173 , pp. 507-513
    • Sloane, D.L.1
  • 38
    • 0002452464 scopus 로고
    • Data collection and processing
    • eds Sawyer, L., Isaacs, N. Baily, S. (Science and Engineering Research Council, Daresbury Laboratory, Daresbury, England)
    • Otwinowski, Z. Data collection and processing. in Proceedings of the CCP4 Study Weekend: Data Collection and Processing (eds Sawyer, L., Isaacs, N.& Baily, S.) 56-62 (Science and Engineering Research Council, Daresbury Laboratory, Daresbury, England, 1993).
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 39
    • 1842391953 scopus 로고    scopus 로고
    • Phases
    • eds Carter, C. Sweet, R. (Academic Press, Orlando)
    • Furey, W. & Swamintha, S. PHASES. in Macromolecular crystallography Vol. 276 (eds Carter, C. & Sweet, R.) (Academic Press, Orlando, 1996).
    • (1996) Macromolecular Crystallography , vol.276
    • Furey, W.1    Swamintha, S.2
  • 40
    • 0000349975 scopus 로고
    • MOLOC: A molecular modeling program
    • Muller, K. MOLOC: A molecular modeling program. Bull. Soc. Chim. 97, 655-667 (1988).
    • (1988) Bull. Soc. Chim. , vol.97 , pp. 655-667
    • Muller, K.1
  • 42
  • 43
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacical and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. & Honig, B. Protein folding and association: insights from the interfacical and thermodynamic properties of hydrocarbons. Proteins 11, 281-296 (1991).
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3


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