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Volumn 48, Issue 26, 2009, Pages 6259-6267

Mechanistic investigations of human reticulocyte 15- and platelet 12-lipoxygenases with arachidonic acid

Author keywords

[No Author keywords available]

Indexed keywords

15-LIPOXYGENASE; ALLOSTERIC EFFECTORS; ARACHIDONIC ACIDS; C-H BOND; CANCEROUS TISSUES; CATALYTIC MECHANISMS; HYDROGEN ATOM ABSTRACTION; LINOLEIC ACID; LIPOXYGENASE; LIPOXYGENASES; OXYGEN CONCENTRATIONS; RATE LIMITING; RATE-LIMITING STEPS; REACTION MECHANISM; RELATIVE ACTIVITIES; SOLVENT ISOTOPE EFFECTS; SUBSTRATE SPECIFICITY; TUNNELING MECHANISM; VARIABLE TEMPERATURE;

EID: 67650094037     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802332j     Document Type: Article
Times cited : (42)

References (43)
  • 1
    • 0031279963 scopus 로고    scopus 로고
    • New insights from spectroscopy into the structure/function relationships of lipoxygenases
    • Solomon, E. I., Zhou, J., Neese, F., and Pavel, E. G. (1997) New insights from spectroscopy into the structure/function relationships of lipoxygenases. Chem. Biol. 4, 795-808.
    • (1997) Chem. Biol. , vol.4 , pp. 795-808
    • Solomon, E.I.1    Zhou, J.2    Neese, F.3    Pavel, E.G.4
  • 2
    • 0028349403 scopus 로고
    • Lipoxin biosynthesis and its impact in inflammatory and vascular events
    • Serhan, C. N. (1994) Lipoxin biosynthesis and its impact in inflammatory and vascular events. Biochim. Biophys. Acta 1212, 1-25.
    • (1994) Biochim. Biophys. Acta , vol.1212 , pp. 1-25
    • Serhan, C.N.1
  • 4
    • 0032573175 scopus 로고    scopus 로고
    • Inhibition of arachidonate 5-lipoxygenase triggers massive apoptosis in human prostate cancer cells
    • Ghosh, J., and Myers, C. E. (1998) Inhibition of arachidonate 5-lipoxygenase triggers massive apoptosis in human prostate cancer cells. Proc. Natl. Acad. Sci. U.S.A. 95, 13182-13187.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13182-13187
    • Ghosh, J.1    Myers, C.E.2
  • 6
    • 0027957514 scopus 로고
    • Epidermis contains platelet-type 12-lipoxygenase that is overexpressed in germinal layer keratinocytes in psoriasis
    • Hussain, H., Shornick, L. P., Shannon, V. R., Wilson, J. D., Funk, C. D., Pentland, A. P., and Holtzman, M. J. (1994) Epidermis contains platelet-type 12-lipoxygenase that is overexpressed in germinal layer keratinocytes in psoriasis. Am. J. Physiol. 266, C243-C253.
    • (1994) Am. J. Physiol. , vol.266
    • Hussain, H.1    Shornick, L.P.2    Shannon, V.R.3    Wilson, J.D.4    Funk, C.D.5    Pentland, A.P.6    Holtzman, M.J.7
  • 7
    • 0032561157 scopus 로고    scopus 로고
    • Enhanced angiogenesis and growth of 12-lipoxygenase gene-transfected MCF-7 human breast cancer cells in athymic nude mice
    • DOI 10.1016/S0304-3835(98)00171-2, PII S0304383598001712
    • Connolly, J. M., and Rose, D. P. (1998) Enhanced angiogenesis and growth of 12-lipoxygenase gene-transfected MCF-7 human breast cancer cells in athymic nude mice. Cancer Lett. 132, 107-112. (Pubitemid 28535191)
    • (1998) Cancer Letters , vol.132 , Issue.1-2 , pp. 107-112
    • Connolly, J.M.1    Rose, D.P.2
  • 8
    • 0032496439 scopus 로고    scopus 로고
    • Role of lipoxygenases in breast cancer
    • Natarajan, R., and Nadler, J. (1998) Role of lipoxygenases in breast cancer. Front. Biosci. 3, E81-E88.
    • (1998) Front. Biosci. , vol.3
    • Natarajan, R.1    Nadler, J.2
  • 9
    • 0033812812 scopus 로고    scopus 로고
    • Overexpression of 15-lipoxygenase in vascular endothelium accelerates early atherosclerosis in LDL receptor-deficient mice
    • Harats, D., Shaish, A., George, J., Mulkins, M., Kurihara, H., Levkovitz, H., and Sigal, E. (2000) Overexpression of 15-lipoxygenase in vascular endothelium accelerates early atherosclerosis in LDL receptor-deficient mice. Arterioscler. Thromb. Vasc. Biol. 20, 2100-2105.
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 2100-2105
    • Harats, D.1    Shaish, A.2    George, J.3    Mulkins, M.4    Kurihara, H.5    Levkovitz, H.6    Sigal, E.7
  • 10
    • 0032555569 scopus 로고    scopus 로고
    • Expression of 15-lipoxygenase by human colorectal carcinoma Caco-2 cells during apoptosis and cell differentiation
    • Kamitani, H., Geller, M., and Eling, T. (1998) Expression of 15-lipoxygenase by human colorectal carcinoma Caco-2 cells during apoptosis and cell differentiation. J. Biol. Chem. 273, 21569-21577.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21569-21577
    • Kamitani, H.1    Geller, M.2    Eling, T.3
  • 12
    • 0033950982 scopus 로고    scopus 로고
    • 2
    • Butler, R. M., S. H., Tindall, D. J., and Young, C. Y. (2000) Nonapoptotic cell death associated with S-phase arrest of prostate cancer cells via the peroxisome proliferator-activated receptor gamma ligand, 15-deoxy-Δ12,14-prostaglandin J2. Cell Growth Differ. 11, 49-61. (Pubitemid 30078666)
    • (2000) Cell Growth and Differentiation , vol.11 , Issue.1 , pp. 49-61
    • Butler, R.1    Mitchell, S.H.2    Tindall, D.J.3    Young, C.Y.F.4
  • 13
    • 0035860789 scopus 로고    scopus 로고
    • 15-Lipoxygenase-1 metabolites down-regulate peroxisome proliferator-activated receptor γ via the MAPK signaling pathway
    • Hsi, L. C., Wilson, L., Nixon, J., and Eling, T. E. (2001) 15-Lipoxygenase-1 metabolites down-regulate peroxisome proliferator-activated receptor γ via the MAPK signaling pathway. J. Biol. Chem. 276, 34545-34552.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34545-34552
    • Hsi, L.C.1    Wilson, L.2    Nixon, J.3    Eling, T.E.4
  • 14
    • 47249091900 scopus 로고    scopus 로고
    • Substrate specificity changes for human reticulocyte and epithelial 15-lipoxygenases reveal allosteric product regulation
    • DOI 10.1021/bi800550n
    • Wecksler, A. T., Kenyon, V., Deschamps, J. D., and Holman, T. R. (2008) Substrate specificity changes for human reticulocyte and epithelial 15-lipoxygenases reveal allosteric product regulation. Biochemistry 47, 7364-7375. (Pubitemid 351991015)
    • (2008) Biochemistry , vol.47 , Issue.28 , pp. 7364-7375
    • Wecksler, A.T.1    Kenyon, V.2    Deschamps, J.D.3    Holman, T.R.4
  • 16
    • 0033571064 scopus 로고    scopus 로고
    • Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase
    • Kilty, I., Logan, A., and Vickers, P. J. (1999) Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase. Eur. J. Biochem. 266, 83-93.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 83-93
    • Kilty, I.1    Logan, A.2    Vickers, P.J.3
  • 17
    • 5444269066 scopus 로고    scopus 로고
    • Tryptophan 500 and arginine 707 define product and substrate active site binding in soybean lipoxygenase-1
    • DOI 10.1021/bi0489098
    • Ruddat, V. C., Mogul, R., Chorny, I., Chen, C., Perrin, N., Whitman, S., Kenyon, V., Jacobson, M. P., Bernasconi, C. F., and Holman, T. R. (2004) Tryptophan 500 and arginine 707 define product and substrate active site binding in soybean lipoxygenase-1. Biochemistry 43, 13063-13071. (Pubitemid 39362776)
    • (2004) Biochemistry , vol.43 , Issue.41 , pp. 13063-13071
    • Ruddat, V.C.1    Mogul, R.2    Chorny, I.3    Chen, C.4    Perrin, N.5    Whitman, S.6    Kenyon, V.7    Jacobson, M.P.8    Bernasconi, C.F.9    Holman, T.R.10
  • 18
    • 0029843150 scopus 로고    scopus 로고
    • Lipoxygenase reaction mechanism: Demonstration that hydrogen abstraction from substrate precedes dioxygen binding during catalytic turnover
    • Glickman, M. H., and Klinman, J. P. (1996) Lipoxygenase reaction mechanism: Demonstration that hydrogen abstraction from substrate precedes dioxygen binding during catalytic turnover. Biochemistry 35, 12882-12892.
    • (1996) Biochemistry , vol.35 , pp. 12882-12892
    • Glickman, M.H.1    Klinman, J.P.2
  • 19
    • 0028864344 scopus 로고
    • Nature of rate-limiting steps in the soybean lipoxygenase-1 reaction
    • Glickman, M. H., and Klinman, J. P. (1995) Nature of rate-limiting steps in the soybean lipoxygenase-1 reaction. Biochemistry 34, 14077-14092.
    • (1995) Biochemistry , vol.34 , pp. 14077-14092
    • Glickman, M.H.1    Klinman, J.P.2
  • 20
    • 0033592315 scopus 로고    scopus 로고
    • Nature of hydrogen transfer in soybean lipoxygenase 1: Separation of primary and secondary isotope effects
    • Rickert, K. W., and Klinman, J. P. (1999) Nature of hydrogen transfer in soybean lipoxygenase 1: Separation of primary and secondary isotope effects. Biochemistry 38, 12218-12228. (Pubitemid 129516190)
    • (1999) Biochemistry , vol.38 , Issue.38 , pp. 12218-12228
    • Rickert, K.W.1    Klinman, J.P.2
  • 21
    • 0037544162 scopus 로고    scopus 로고
    • Kinetic investigations of the rate-limiting step in human 12- And 15-lipoxygenase
    • DOI 10.1021/bi0273462
    • Segraves, E. N., and Holman, T. R. (2003) Kinetic investigations of the rate-limiting step in human 12- and 15-lipoxygenase. Biochemistry 42, 5236-5243. (Pubitemid 36560419)
    • (2003) Biochemistry , vol.42 , Issue.18 , pp. 5236-5243
    • Segraves, E.N.1    Holman, T.R.2
  • 22
    • 55249126573 scopus 로고    scopus 로고
    • Kinetic isotope effects in the oxidation of arachidonic acid by soybean lipoxygenase-1
    • Jacquot, C., Peng, S., and van der Donk, W. A. (2008) Kinetic isotope effects in the oxidation of arachidonic acid by soybean lipoxygenase-1. Bioorg. Med. Chem. Lett. 18, 5959-5962.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 5959-5962
    • Jacquot, C.1    Peng, S.2    Van Der Donk, W.A.3
  • 23
    • 46849094690 scopus 로고    scopus 로고
    • Isotope sensitive branching and kinetic isotope effects in the reaction of deuterated arachidonic acids with human 12- And 15-lipoxygenases
    • DOI 10.1021/bi800308q
    • Jacquot, C., Wecksler, A. T., McGinley, C. M., Segraves, E. N., Holman, T. R., and van der Donk, W. A. (2008) Isotope sensitive branching and kinetic isotope effects in the reaction of deuterated arachidonic acids with human 12- and 15-lipoxygenases. Biochemistry 47, 7295-7303. (Pubitemid 351956378)
    • (2008) Biochemistry , vol.47 , Issue.27 , pp. 7295-7303
    • Jacquot, C.1    Wecksler, A.T.2    McGinley, C.M.3    Segraves, E.N.4    Holman, T.R.5    Van Der Donk, W.A.6
  • 24
    • 0033576983 scopus 로고    scopus 로고
    • Large Competitive Kinetic Isotope Effects in Human 15-Lipoxygenase Catalysis Measured by a Novel HPLC Method
    • Lewis, E., Johnson, E., and Holman, T. (1999) Large Competitive Kinetic Isotope Effects in Human 15-Lipoxygenase Catalysis Measured by a Novel HPLC Method. J. Am. Chem. Soc. 121, 1395-1396.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 1395-1396
    • Lewis, E.1    Johnson, E.2    Holman, T.3
  • 25
    • 0037063567 scopus 로고    scopus 로고
    • Synthesis of isotopically labeled arachidonic acids to probe the reaction mechanism of prostaglandin H synthase
    • Peng, S., Okeley, N. M., Tsai, A. L., Wu, G., Kulmacz, R. J., and van der Donk, W. A. (2002) Synthesis of isotopically labeled arachidonic acids to probe the reaction mechanism of prostaglandin H synthase. J. Am. Chem. Soc. 124, 10785-10796.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10785-10796
    • Peng, S.1    Okeley, N.M.2    Tsai, A.L.3    Wu, G.4    Kulmacz, R.J.5    Van Der Donk, W.A.6
  • 26
    • 1342306678 scopus 로고    scopus 로고
    • Synthesis of site-specifically labeled arachidonic acids as mechanistic probes for prostaglandin H synthase
    • Peng, S., McGinley, C. M., and van der Donk, W. A. (2004) Synthesis of site-specifically labeled arachidonic acids as mechanistic probes for prostaglandin H synthase. Org. Lett. 6, 349-352.
    • (2004) Org. Lett. , vol.6 , pp. 349-352
    • Peng, S.1    McGinley, C.M.2    Van Der Donk, W.A.3
  • 27
    • 0037332097 scopus 로고    scopus 로고
    • Exploring sponge-derived terpenoids for their potency and selectivity against 12-human, 15-human, and 15-soybean lipoxygenases
    • Amagata, T., Whitman, S., Johnson, T. A., Stessman, C. C., Loo, C. P., Lobkovsky, E., Clardy, J., Crews, P., and Holman, T. R. (2003) Exploring sponge-derived terpenoids for their potency and selectivity against 12-human, 15-human, and 15-soybean lipoxygenases. J. Nat. Prod. 66, 230-235.
    • (2003) J. Nat. Prod. , vol.66 , pp. 230-235
    • Amagata, T.1    Whitman, S.2    Johnson, T.A.3    Stessman, C.C.4    Loo, C.P.5    Lobkovsky, E.6    Clardy, J.7    Crews, P.8    Holman, T.R.9
  • 28
    • 0027196413 scopus 로고
    • Purification and characterization of recombinant histidine-tagged human platelet 12-lipoxygenase expressed in a baculovirus/insect cell system
    • Chen, X. S., Brash, A. R., and Funk, C. D. (1993) Purification and characterization of recombinant histidine-tagged human platelet 12-lipoxygenase expressed in a baculovirus/insect cell system. Eur. J. Biochem. 214, 845-852.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 845-852
    • Chen, X.S.1    Brash, A.R.2    Funk, C.D.3
  • 29
    • 41249086003 scopus 로고    scopus 로고
    • Detection and Quantitation of Eicosanoids via High Performance Liquid Chromatography-Electrospray Ionization-Mass Spectrometry
    • Deems, R., Buczynski, M. W., Bowers-Gentry, R., Harkewicz, R., and Dennis, E. A. (2007) Detection and Quantitation of Eicosanoids via High Performance Liquid Chromatography-Electrospray Ionization-Mass Spectrometry. Methods Enzymol. 432, 59-82.
    • (2007) Methods Enzymol. , vol.432 , pp. 59-82
    • Deems, R.1    Buczynski, M.W.2    Bowers-Gentry, R.3    Harkewicz, R.4    Dennis, E.A.5
  • 30
    • 0141706648 scopus 로고    scopus 로고
    • Kinetic studies of oxygen reactivity in soybean lipoxygenase-1
    • DOI 10.1021/bi0300884
    • Knapp, M. J., and Klinman, J. P. (2003) Kinetic studies of oxygen reactivity in soybean lipoxygenase-1. Biochemistry 42, 11466-11475. (Pubitemid 37205741)
    • (2003) Biochemistry , vol.42 , Issue.39 , pp. 11466-11475
    • Knapp, M.J.1    Klinman, J.P.2
  • 31
    • 0037123216 scopus 로고    scopus 로고
    • Temperature-dependent isotope effects in soybean lipoxygenase-1: Correlating hydrogen tunneling with protein dynamics
    • Knapp, M. J., Rickert, K., and Klinman, J. P. (2002) Temperature- dependent isotope effects in soybean lipoxygenase-1: Correlating hydrogen tunneling with protein dynamics. J. Am. Chem. Soc. 124, 3865-3874.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3865-3874
    • Knapp, M.J.1    Rickert, K.2    Klinman, J.P.3
  • 32
    • 0035794224 scopus 로고    scopus 로고
    • Importance of barrier shape in enzyme-catalyzed reactions. Vibrationally assisted hydrogen tunneling in tryptophan tryptophylquinone-dependent amine dehydrogenases
    • Basran, J., Patel, S., Sutcliffe, M. J., and Scrutton, N. S. (2001) Importance of barrier shape in enzyme-catalyzed reactions. Vibrationally assisted hydrogen tunneling in tryptophan tryptophylquinone-dependent amine dehydrogenases. J. Biol. Chem. 276, 6234-6242.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6234-6242
    • Basran, J.1    Patel, S.2    Sutcliffe, M.J.3    Scrutton, N.S.4
  • 34
    • 63849211644 scopus 로고    scopus 로고
    • Analysis of Kinetic Isotope Effects for Proton-Coupled Electron Transfer Reactions
    • Edwards, S. J., Soudackov, A. V., and Hammes-Schiffer, S. (2009) Analysis of Kinetic Isotope Effects for Proton-Coupled Electron Transfer Reactions. J. Phys. Chem. A 113, 2117-2126.
    • (2009) J. Phys. Chem. A , vol.113 , pp. 2117-2126
    • Edwards, S.J.1    Soudackov, A.V.2    Hammes-Schiffer, S.3
  • 35
    • 11344269742 scopus 로고    scopus 로고
    • Kinetic Isotope Effects for Nonadiabatic Proton Transfer Reactions in a Polar Environment. 1. Interpretation of Tunneling Kinetic Isotopic Effects
    • Kiefer, P. M., and Hynes, J. T. (2004) Kinetic Isotope Effects for Nonadiabatic Proton Transfer Reactions in a Polar Environment. 1. Interpretation of Tunneling Kinetic Isotopic Effects. J. Phys. Chem. A 108, 11793-11808.
    • (2004) J. Phys. Chem. A , vol.108 , pp. 11793-11808
    • Kiefer, P.M.1    Hynes, J.T.2
  • 36
    • 0037149128 scopus 로고    scopus 로고
    • A Theory that Connects Proton-Coupled Electron-Transfer and Hydrogen-Atom Transfer Reactions
    • Cukier, R. I. (2002) A Theory that Connects Proton-Coupled Electron-Transfer and Hydrogen-Atom Transfer Reactions. J. Phys. Chem. B 106, 1746-1757.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 1746-1757
    • Cukier, R.I.1
  • 39
    • 0033837450 scopus 로고    scopus 로고
    • Structural basis for the positional specificity of lipoxygenases
    • DOI 10.1016/S0090-6980(00)00084-8, PII S0090698000000848
    • Kuhn, H. (2000) Structural basis for the positional specificity of lipoxygenases. Prostaglandins Other Lipid Mediators 62, 255-270. (Pubitemid 30645921)
    • (2000) Prostaglandins and Other Lipid Mediators , vol.62 , Issue.3 , pp. 255-270
    • Kuhn, H.1
  • 40
    • 0041866686 scopus 로고    scopus 로고
    • An unusual isotope effect on substrate inhibition in the oxidation of arachidonic acid by lipoxygenase
    • Peng, S., and van der Donk, W. A. (2003) An unusual isotope effect on substrate inhibition in the oxidation of arachidonic acid by lipoxygenase. J. Am. Chem. Soc. 125, 8988-8989.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8988-8989
    • Peng, S.1    Van Der Donk, W.A.2
  • 41
    • 0033616453 scopus 로고    scopus 로고
    • Mathematical model of oxygen transport in the cerebral cortex
    • DOI 10.1016/S0006-8993(98)01200-1, PII S0006899398012001
    • Hudetz, A. G. (1999) Mathematical model of oxygen transport in the cerebral cortex. Brain Res. 817, 75-83. (Pubitemid 29225347)
    • (1999) Brain Research , vol.817 , Issue.1-2 , pp. 75-83
    • Hudetz, A.G.1
  • 43
    • 34548060346 scopus 로고    scopus 로고
    • Molecular dioxygen enters the active site of 12/15-lipoxygenase via dynamic oxygen access channels
    • Saam, J., Ivanov, I., Walther, M., Holzhutter, H. G., and Kuhn, H. (2007) Molecular dioxygen enters the active site of 12/15-lipoxygenase via dynamic oxygen access channels. Proc. Natl. Acad. Sci. U.S. A. 104, 13319-13324.
    • (2007) Proc. Natl. Acad. Sci. U.S. A. , vol.104 , pp. 13319-13324
    • Saam, J.1    Ivanov, I.2    Walther, M.3    Holzhutter, H.G.4    Kuhn, H.5


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