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Volumn 1841, Issue 1, 2014, Pages 1-10

Probing conformational changes in lipoxygenases upon membrane binding: Fine-tuning by the active site inhibitor ETYA

Author keywords

Fluorescence dynamics; High pressure; Lipoxygenases; Motional flexibility

Indexed keywords

5,8,11,14 ICOSATETRAYNOIC ACID; LIPOXYGENASE;

EID: 84885540914     PISSN: 13881981     EISSN: 18792618     Source Type: Journal    
DOI: 10.1016/j.bbalip.2013.08.015     Document Type: Article
Times cited : (10)

References (39)
  • 1
    • 70349501375 scopus 로고    scopus 로고
    • Linking new paradigms in protein chemistry to reversible membrane-protein interactions
    • Ø. Halskau, A. Muga, and A. Martinez Linking new paradigms in protein chemistry to reversible membrane-protein interactions Curr. Prot. Pept. Sci. 10 2009 339 359
    • (2009) Curr. Prot. Pept. Sci. , vol.10 , pp. 339-359
    • Halskau Ø1    Muga, A.2    Martinez, A.3
  • 2
    • 80054052917 scopus 로고    scopus 로고
    • Lipoxygenase and leukotriene pathways: Biochemistry, biology and roles in disease
    • J.Z. Haeggström, and C.D. Funk Lipoxygenase and leukotriene pathways: biochemistry, biology and roles in disease Chem. Rev. 111 2011 5866 5898
    • (2011) Chem. Rev. , vol.111 , pp. 5866-5898
    • Haeggström, J.Z.1    Funk, C.D.2
  • 3
    • 0034624019 scopus 로고    scopus 로고
    • The N-terminal domain of 5-lipoxygenase binds calcium and mediates calcium stimulation of enzyme activity
    • DOI 10.1074/jbc.M006136200
    • T. Hammarberg, P. Provost, B. Persson, and O. Rådmark The N-terminal domain of 5-lipoxygenase binds calcium and mediates calcium stimulation of enzyme activity J. Biol. Chem. 275 2000 38787 38793 (Pubitemid 32009215)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.49 , pp. 38787-38793
    • Hammarberg, T.1    Provost, P.2    Persson, B.3    Radmark, O.4
  • 4
    • 0037066761 scopus 로고    scopus 로고
    • Molecular basis of the specific subcellular localization of the C2-like domain of 5-lipoxygenase
    • DOI 10.1074/jbc.M112393200
    • S. Kulkarni, S. Das, C.D. Funk, D. Murray, and W. Cho Molecular basis of the specific subcellular localization of the C2-like domain of 5-lipoxygenase J. Biol. Chem. 277 2002 13167 13174 (Pubitemid 34952687)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 13167-13174
    • Kulkarni, S.1    Das, S.2    Funk, C.D.3    Murray, D.4    Cho, W.5
  • 5
    • 77952312969 scopus 로고    scopus 로고
    • Regulation of the activity of 5-lipoxygenase, a key enzyme in leukotriene biosynthesis
    • O. Rådmark, and B. Samuelsson Regulation of the activity of 5-lipoxygenase, a key enzyme in leukotriene biosynthesis Biochem. Biophys. Res. Commun. 396 2010 105 110
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 105-110
    • Rådmark, O.1    Samuelsson, B.2
  • 6
    • 0031975571 scopus 로고    scopus 로고
    • Membrane translocation of 15-lipoxygenase in hematopoietic cells is calcium-dependent and activates the oxygenase activity of the enzyme
    • R. Brinckmann, K. Schnurr, D. Heydeck, T. Rosenbach, G. Kolde, and H. Kühn Membrane translocation of 15-lipoxygenase in hematopoietic cells is calcium-dependent and activates the oxygenase activity of the enzyme Blood 91 1998 64 74 (Pubitemid 28018730)
    • (1998) Blood , vol.91 , Issue.1 , pp. 64-74
    • Brinckmann, R.1    Schnurr, K.2    Heydeck, D.3    Rosenbach, T.4    Kolde, G.5    Kuhn, H.6
  • 7
    • 70350507480 scopus 로고    scopus 로고
    • Enzymes in jasmonate biosynthesis - Structure, function, regulation
    • A. Schaller, and A. Stintzi Enzymes in jasmonate biosynthesis - structure, function, regulation Phytochemistry 70 2009 1532 1538
    • (2009) Phytochemistry , vol.70 , pp. 1532-1538
    • Schaller, A.1    Stintzi, A.2
  • 8
    • 0027246677 scopus 로고
    • The three-dimensional structure of an arachidonic acid 15-lipoxygenase
    • J.C. Boyington, B.J. Gaffney, and L.M. Amzel The three-dimensional structure of an arachidonic acid 15-lipoxygenase Science 260 1993 1482 1486 (Pubitemid 23273261)
    • (1993) Science , vol.260 , Issue.5113 , pp. 1482-1486
    • Boyington, J.C.1    Gaffney, B.J.2    Amzel, L.M.3
  • 9
    • 0029740369 scopus 로고    scopus 로고
    • Crystal structure of soybean lipoxygenase L-1 at 1.4 A resolution
    • DOI 10.1021/bi960576u
    • W. Minor, J. Steczko, B. Stec, Z. Otwinowski, J.T. Bolin, R. Walter, and B. Axelrod Crystal structure of soybean lipoxygenase L-1 at 1.4 Å resolution Biochemistry 35 1996 10687 10701 (Pubitemid 26279648)
    • (1996) Biochemistry , vol.35 , Issue.33 , pp. 10687-10701
    • Minor, W.1    Steczko, J.2    Stec, B.3    Otwinowski, Z.4    Bolin, J.T.5    Walter, R.6    Axelrod, B.7
  • 10
    • 0030736867 scopus 로고    scopus 로고
    • The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity
    • S.A. Gillmor, A. Villaseñor, R. Fletterick, E. Sigal, and M.F. Browner The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity Nat. Struct. Biol. 4 1997 1003 1009 (Pubitemid 27525804)
    • (1997) Nature Structural Biology , vol.4 , Issue.12 , pp. 1003-1009
    • Gillmor, S.A.1    Villasenor, A.2    Fletterick, R.3    Sigal, E.4    Browner, M.F.5
  • 11
    • 69049086852 scopus 로고    scopus 로고
    • The 1.85 Å structure of an 8R-lipoxygenase suggests a general model for lipoxygenase product specificity
    • D.B. Neau, N.C. Gilbert, S.G. Bartlett, W. Boeglin, A.R. Brash, and M.E. Newcomer The 1.85 Å structure of an 8R-lipoxygenase suggests a general model for lipoxygenase product specificity Biochemistry 48 2009 7906 7915
    • (2009) Biochemistry , vol.48 , pp. 7906-7915
    • Neau, D.B.1    Gilbert, N.C.2    Bartlett, S.G.3    Boeglin, W.4    Brash, A.R.5    Newcomer, M.E.6
  • 13
    • 84862661138 scopus 로고    scopus 로고
    • Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca2 + regulation
    • P. Eek, R. Järving, I. Järving, N.C. Gilbert, M.E. Newcomer, and N. Samel Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca2 + regulation J. Biol. Chem. 287 2012 22377 22386
    • (2012) J. Biol. Chem. , vol.287 , pp. 22377-22386
    • Eek, P.1    Järving, R.2    Järving, I.3    Gilbert, N.C.4    Newcomer, M.E.5    Samel, N.6
  • 14
    • 5144223918 scopus 로고    scopus 로고
    • Structural flexibility of the N-terminal β-barrel domain of 15-Lipoxygenase-1 probed by small angle x-ray scattering. Functional consequences for activity regulation and membrane binding
    • DOI 10.1016/j.jmb.2004.08.076, PII S0022283604010769
    • M. Hammel, M. Walther, R. Prassl, and H. Kühn Structural flexibility of the N-terminal beta-barrel domain of 15-lipoxygenase-1 probed by small angle X-ray scattering. Functional consequences for activity regulation and membrane binding J. Mol. Biol. 343 2004 917 929 (Pubitemid 39345953)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.4 , pp. 917-929
    • Hammel, M.1    Walther, M.2    Prassl, R.3    Kuhn, H.4
  • 17
    • 50849087043 scopus 로고    scopus 로고
    • Structural properties of plant and mammalian lipoxygenases. Temperature-dependent conformational alterations and membrane binding ability
    • G. Mei, A. Di Venere, E. Nicolai, C.B. Angelucci, I. Ivanov, A. Sabatucci, E. Dainese, H. Kühn, and M. Maccarrone Structural properties of plant and mammalian lipoxygenases. Temperature-dependent conformational alterations and membrane binding ability Biochemistry 47 2008 9234 9242
    • (2008) Biochemistry , vol.47 , pp. 9234-9242
    • Mei, G.1    Di Venere, A.2    Nicolai, E.3    Angelucci, C.B.4    Ivanov, I.5    Sabatucci, A.6    Dainese, E.7    Kühn, H.8    Maccarrone, M.9
  • 18
    • 38549129314 scopus 로고    scopus 로고
    • Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data
    • DOI 10.1002/prot.21590
    • J. Choi, J.K. Chon, S. Kim, and W. Shin Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data Proteins Struct. Funct. Bioinforma. 70 2008 1023 1032 (Pubitemid 351161958)
    • (2008) Proteins: Structure, Function and Genetics , vol.70 , Issue.3 , pp. 1023-1032
    • Choi, J.1    Jae, K.C.2    Kim, S.3    Shin, W.4
  • 19
    • 81355160490 scopus 로고    scopus 로고
    • The N-terminal β-barrel domain of mammalian lipoxygenases including mouse 5-lipoxygenase is not essential for catalytic activity and membrane binding but exhibits regulatory functions
    • M. Walther, K. Hofheinz, R. Vogel, J. Roffeis, and H. Kühn The N-terminal β-barrel domain of mammalian lipoxygenases including mouse 5-lipoxygenase is not essential for catalytic activity and membrane binding but exhibits regulatory functions Arch. Biochem. Biophys. 516 2011 1 9
    • (2011) Arch. Biochem. Biophys. , vol.516 , pp. 1-9
    • Walther, M.1    Hofheinz, K.2    Vogel, R.3    Roffeis, J.4    Kühn, H.5
  • 20
    • 77953526759 scopus 로고    scopus 로고
    • A novel role for iron in modulating the activity and membrane-binding ability of a trimmed soybean lipoxygenase-1
    • E. Dainese, C.B. Angelucci, A. Sabatucci, V. De Filippis, G. Mei, and M. Maccarrone A novel role for iron in modulating the activity and membrane-binding ability of a trimmed soybean lipoxygenase-1 FASEB J. 24 2010 1725 1736
    • (2010) FASEB J. , vol.24 , pp. 1725-1736
    • Dainese, E.1    Angelucci, C.B.2    Sabatucci, A.3    De Filippis, V.4    Mei, G.5    Maccarrone, M.6
  • 23
    • 77952093185 scopus 로고    scopus 로고
    • Quantification of protein-lipid selectivity using FRET
    • L.M. Loura, M. Prieto, and F. Fernandes Quantification of protein-lipid selectivity using FRET Eur. Biophys. J. 39 2010 565 578
    • (2010) Eur. Biophys. J. , vol.39 , pp. 565-578
    • Loura, L.M.1    Prieto, M.2    Fernandes, F.3
  • 24
    • 0021345198 scopus 로고
    • The mechanism of inactivation of lipoxygenases by acetylenic fatty acids
    • DOI 10.1111/j.1432-1033.1984.tb08044.x
    • H. Kühn, H.G. Holzhütter, T. Schewe, C. Hiebsch, and S.M. Rapoport The mechanism of inactivation of lipoxygenases by acetylenic fatty acids Eur. J. Biochem. 139 1984 577 583 (Pubitemid 14163208)
    • (1984) European Journal of Biochemistry , vol.139 , Issue.3 , pp. 577-583
    • Kuhn, H.1    Holzhutter, H.G.2    Schewe, T.3
  • 25
    • 0038381477 scopus 로고    scopus 로고
    • Structure-to-function relationship of mini-lipoxygenase, a 60-kDa fragment of soybean lipoxygenase-1 with lower stability but higher enzymatic activity
    • DOI 10.1074/jbc.M212122200
    • A. Di Venere, M.L. Salucci, G. van Zadelhoff, G. Veldink, G. Mei, N. Rosato, A. Finazzi-Agrò, and M. Maccarrone Structure-to-function relationship of mini-lipoxygenase, a 60-kDa fragment of soybean lipoxygenase-1 with lower stability but higher enzymatic activity J. Biol. Chem. 278 2003 18281 18288 (Pubitemid 36799447)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.20 , pp. 18281-18288
    • Di Venere, A.1    Salucci, M.L.2    Van Zadelhoff, G.3    Veldink, G.4    Mei, G.5    Rosato, N.6    Finazzi-Agro, A.7    Maccarrone, M.8
  • 26
    • 0942276361 scopus 로고    scopus 로고
    • Investigations into calcium-dependent membrane association of 15-lipoxygenase-1: Mechanistic roles of surface-exposed hydrophobic amino acids and calcium
    • DOI 10.1074/jbc.M309564200
    • M. Walther, R. Wiesner, and H. Kühn Investigations into calcium-dependent membrane association of 15-lipoxygenase-1, mechanistic roles of surface-exposed hydrophobic amino acids and calcium J. Biol. Chem. 279 2004 3717 3725 (Pubitemid 38140615)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.5 , pp. 3717-3725
    • Walther, M.1    Wiesner, R.2    Kuhn, H.3
  • 27
    • 0035478292 scopus 로고    scopus 로고
    • Pressure provides new insights into protein folding, dynamics and structure
    • DOI 10.1016/S0968-0004(01)01949-1, PII S0968000401019491
    • J.L. Silva, D. Foguel, and C.A. Royer Pressure provides new insights into protein folding, dynamics and structure Trends Biochem. Sci. 26 2001 612 618 (Pubitemid 32925191)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.10 , pp. 612-618
    • Silva, J.L.1    Foguel, D.2    Royer, C.A.3
  • 30
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
    • DOI 10.1017/S0033583507004635, PII S0033583507004635
    • C.D. Putnam, M. Hammel, G.L. Hura, and J.A. Tainer X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution Q. Rev. Biophys. 40 2007 191 285 (Pubitemid 350261954)
    • (2007) Quarterly Reviews of Biophysics , vol.40 , Issue.3 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 34
    • 0025845307 scopus 로고
    • Oligomeric protein associations: Transition from stochastic to deterministic equilibrium
    • L. Erijman, and G. Weber Oligomeric protein associations: transition from stochastic to deterministic equilibrium Biochemistry 30 1991 1595 1599
    • (1991) Biochemistry , vol.30 , pp. 1595-1599
    • Erijman, L.1    Weber, G.2
  • 35
    • 0035849587 scopus 로고    scopus 로고
    • Tryptic digestion of soybean lipoxygenase-1 generates a 60 kDA fragment with improved activity and membrane binding ability
    • DOI 10.1021/bi010187m
    • M. Maccarrone, M.L. Salucci, G. van Zadelhoff, F. Malatesta, G. Veldink, J.F. Vliegenthart, and A. Finazzi-Agrò Tryptic digestion of soybean lipoxygenase-1 generates a 60 kDa fragment with improved activity and membrane binding ability Biochemistry 40 2001 6819 6827 (Pubitemid 32538227)
    • (2001) Biochemistry , vol.40 , Issue.23 , pp. 6819-6827
    • Maccarrone, M.1    Salucci, M.L.2    Van Zadelhoff, G.3    Malatesta, F.4    Veldink, G.5    Vliegenthart, J.F.G.6    Finazzi-Agro, A.7
  • 36
    • 0037178834 scopus 로고    scopus 로고
    • The N-terminal domain of the reticulocyte-type 15-lipoxygenase is not essential for enzymatic activity but contains determinants for membrane binding
    • DOI 10.1074/jbc.M203234200
    • M. Walther, M. Anton, M. Wiedmann, R. Fletterick, and H. Kühn The N-terminal domain of the reticulocyte-type 15-lipoxygenase is not essential for enzymatic activity but contains determinants for membrane binding J. Biol. Chem. 277 2002 27360 27366 (Pubitemid 34951756)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 27360-27366
    • Walther, M.1    Anton, M.2    Wiedmann, M.3    Fletterick, R.4    Kuhn, H.5
  • 37
    • 70349334626 scopus 로고    scopus 로고
    • Effect of pressure on membranes
    • R. Winter, and C. Jeworrek Effect of pressure on membranes Soft Matter 5 2009 3157 3173
    • (2009) Soft Matter , vol.5 , pp. 3157-3173
    • Winter, R.1    Jeworrek, C.2
  • 38
    • 33749528137 scopus 로고    scopus 로고
    • Pressure tuning of the morphology of heterogeneous lipid vesicles: A two-photon-excitation fluorescence microscopy study
    • DOI 10.1529/biophysj.106.088716
    • C. Nicolini, A. Celli, E. Gratton, and R. Winter Pressure tuning of the morphology of heterogeneous lipid vesicles: a two-photon-excitation fluorescence microscopy study Biophys. J. 91 2006 2936 2942 (Pubitemid 44526484)
    • (2006) Biophysical Journal , vol.91 , Issue.8 , pp. 2936-2942
    • Nicolini, C.1    Celli, A.2    Gratton, E.3    Winter, R.4
  • 39
    • 84859845957 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy
    • J. Ries, P. Schwille, Fluorescence correlation spectroscopy, Bioessays 34 (2012) 361-368.
    • (2012) Bioessays , vol.34 , pp. 361-368
    • Ries, J.1    Schwille, P.2


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