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Volumn 376, Issue 1, 2008, Pages 193-209

Human Platelet 12-Lipoxygenase, New Findings about Its Activity, Membrane Binding and Low-resolution Structure

Author keywords

fatty acid metabolism; human lipoxygenase; membrane binding; SAXS

Indexed keywords

ARACHIDONATE 12 LIPOXYGENASE; ARACHIDONIC ACID; CYSTEINE; OLIGOMER;

EID: 38049120330     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.11.086     Document Type: Article
Times cited : (60)

References (53)
  • 2
    • 38049129161 scopus 로고    scopus 로고
    • Choi, J., Chon, J. K., Kim, S. & Shin W. (2007). Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data. Proteins: Struct. Funct. Bioinf., in press (Sept. 10; Epub ahead of print).
  • 3
    • 0033607040 scopus 로고    scopus 로고
    • The PLAT domain: a new piece in the PKD1 puzzle
    • Bateman A., and Sandford R. The PLAT domain: a new piece in the PKD1 puzzle. Curr. Biol. 9 (1999) R588-R590
    • (1999) Curr. Biol. , vol.9
    • Bateman, A.1    Sandford, R.2
  • 4
    • 5344241165 scopus 로고    scopus 로고
    • Mass spectrometric methods for the determination of flavonoids in biological samples
    • Prasain J.K., Wang C.C., and Barnes S. Mass spectrometric methods for the determination of flavonoids in biological samples. Free Radic Biol. Med. 37 (2004) 1324-1350
    • (2004) Free Radic Biol. Med. , vol.37 , pp. 1324-1350
    • Prasain, J.K.1    Wang, C.C.2    Barnes, S.3
  • 6
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 8
    • 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
    • Walther M., Anton M., Wiedmann M., Fletterick R., and Kühn H. 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
    • (2002) J. Biol. Chem. , vol.277 , pp. 27360-27366
    • Walther, M.1    Anton, M.2    Wiedmann, M.3    Fletterick, R.4    Kühn, H.5
  • 9
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76 (1999) 2879-2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 10
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small angle scattering
    • Volkov V.V., and Svergun D.I. Uniqueness of ab initio shape determination in small angle scattering. J. Appl. Crystallogr. 36 (2003) 860-864
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 12
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modelling of macromolecular complexes against small-angle scattering data
    • Petoukhov M.V., and Svergun D.I. Global rigid body modelling of macromolecular complexes against small-angle scattering data. Biophys. J. 89 (2005) 1237-1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 13
    • 0031552370 scopus 로고    scopus 로고
    • Determination of atomic desolvation energies from the structures of crystallized proteins
    • Zhang C., Vasmatzis G., Cornette J.L., and DeLisi C. Determination of atomic desolvation energies from the structures of crystallized proteins. J. Mol. Biol. 267 (1997) 707-726
    • (1997) J. Mol. Biol. , vol.267 , pp. 707-726
    • Zhang, C.1    Vasmatzis, G.2    Cornette, J.L.3    DeLisi, C.4
  • 14
    • 0021210519 scopus 로고
    • Subcellular localization and some properties of lipoxygenase activity in human blood platelets
    • Lagarde M., Croset M., Authi K.S., and Crawford N. Subcellular localization and some properties of lipoxygenase activity in human blood platelets. Biochem. J. 222 (1984) 495-500
    • (1984) Biochem. J. , vol.222 , pp. 495-500
    • Lagarde, M.1    Croset, M.2    Authi, K.S.3    Crawford, N.4
  • 15
    • 0019886689 scopus 로고
    • A novel preparation of human platelet lipoxygenase. Characteristics and inhibition by a variety of phenyl hydrazones and comparisons with other lipoxygenases
    • Wallach D.P., and Brown V.R. A novel preparation of human platelet lipoxygenase. Characteristics and inhibition by a variety of phenyl hydrazones and comparisons with other lipoxygenases. Biochim. Biophys. Acta 663 (1981) 361-372
    • (1981) Biochim. Biophys. Acta , vol.663 , pp. 361-372
    • Wallach, D.P.1    Brown, V.R.2
  • 16
    • 38049168986 scopus 로고
    • Cahkvin L.W., and Bailey D.M. (Eds), Academic Press, New York
    • Aharony D., Smith J.B., and Sliver M.J. In: Cahkvin L.W., and Bailey D.M. (Eds). The Leukotrienes (1984), Academic Press, New York
    • (1984) The Leukotrienes
    • Aharony, D.1    Smith, J.B.2    Sliver, M.J.3
  • 18
    • 0034811728 scopus 로고    scopus 로고
    • Steric control of oxygenation regiochemistry in soybean lipoxygenase-1
    • Knapp M.J., Seebeck F.P., and Klinman J.P. Steric control of oxygenation regiochemistry in soybean lipoxygenase-1. J. Am. Chem. Soc. 123 (2001) 2931-2932
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2931-2932
    • Knapp, M.J.1    Seebeck, F.P.2    Klinman, J.P.3
  • 19
    • 0035954384 scopus 로고    scopus 로고
    • Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1
    • Tomchick D.R., Phan P., Cymborowski M., Minor W., and Holman T.R. Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1. Biochemistry 40 (2001) 7509-7517
    • (2001) Biochemistry , vol.40 , pp. 7509-7517
    • Tomchick, D.R.1    Phan, P.2    Cymborowski, M.3    Minor, W.4    Holman, T.R.5
  • 21
    • 0022869485 scopus 로고
    • Arachidonate 12-lipoxygenase purified from porcine leukocytes by immunoaffinity chromatography and its reactivity with hydroperoxyeicosatetraenoic acids
    • Yokoyama C., Shinjo F., Yoshimoto T., Yamamoto S., Oates J.A., and Brash A.R. Arachidonate 12-lipoxygenase purified from porcine leukocytes by immunoaffinity chromatography and its reactivity with hydroperoxyeicosatetraenoic acids. J. Biol. Chem. 261 (1986) 16714-16721
    • (1986) J. Biol. Chem. , vol.261 , pp. 16714-16721
    • Yokoyama, C.1    Shinjo, F.2    Yoshimoto, T.3    Yamamoto, S.4    Oates, J.A.5    Brash, A.R.6
  • 22
    • 0037544162 scopus 로고    scopus 로고
    • Kinetic investigations of the rate-limiting step in human 12- and 15-lipoxygenase
    • Segraves E.N., and Holman T.R. Kinetic investigations of the rate-limiting step in human 12- and 15-lipoxygenase. Biochemistry 42 (2003) 5236-5243
    • (2003) Biochemistry , vol.42 , pp. 5236-5243
    • Segraves, E.N.1    Holman, T.R.2
  • 23
    • 0027166718 scopus 로고
    • Structure-function properties of human platelet 12-lipoxygenase: chimeric enzyme and in vitro mutagenesis studies
    • Chen X.S., and Funk C.D. Structure-function properties of human platelet 12-lipoxygenase: chimeric enzyme and in vitro mutagenesis studies. FASEB J. 7 (1993) 694-701
    • (1993) FASEB J. , vol.7 , pp. 694-701
    • Chen, X.S.1    Funk, C.D.2
  • 24
    • 0029991455 scopus 로고    scopus 로고
    • Suicide inactivation of porcine leukocyte 12-lipoxygenase associated with its incorporation of 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid derivative
    • Kishimoto K., Nakamura M., Suzuki H., Yoshimoto T., Yamamoto S., Takao T., et al. Suicide inactivation of porcine leukocyte 12-lipoxygenase associated with its incorporation of 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid derivative. Biochim. Biophys. Acta 1300 (1996) 56-62
    • (1996) Biochim. Biophys. Acta , vol.1300 , pp. 56-62
    • Kishimoto, K.1    Nakamura, M.2    Suzuki, H.3    Yoshimoto, T.4    Yamamoto, S.5    Takao, T.6
  • 25
    • 0035836521 scopus 로고    scopus 로고
    • Inhibition studies of soybean and human 15-lipoxygenases with long-chain alkenyl sulfate substrates
    • Mogul R., and Holman T.R. Inhibition studies of soybean and human 15-lipoxygenases with long-chain alkenyl sulfate substrates. Biochemistry 40 (2001) 4391-4397
    • (2001) Biochemistry , vol.40 , pp. 4391-4397
    • Mogul, R.1    Holman, T.R.2
  • 26
    • 0033844705 scopus 로고    scopus 로고
    • Iron release from the active site of lipoxygenase
    • Fuchs C., and Spiteller G. Iron release from the active site of lipoxygenase. Z. Naturforsch. 55c (2000) 643-648
    • (2000) Z. Naturforsch. , vol.55 c , pp. 643-648
    • Fuchs, C.1    Spiteller, G.2
  • 27
    • 0034805399 scopus 로고    scopus 로고
    • Iron extraction from soybean lipoxygenase 3 and reconstitution of catalytic activity from the apoenzyme
    • Kariapper M.S., Dunham W.R., and Funk Jr. M.O. Iron extraction from soybean lipoxygenase 3 and reconstitution of catalytic activity from the apoenzyme. Biochem. Biophys. Res. Commun. 284 (2001) 563-567
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 563-567
    • Kariapper, M.S.1    Dunham, W.R.2    Funk Jr., M.O.3
  • 28
    • 27544477825 scopus 로고    scopus 로고
    • Structural biology of mammalian lipoxygenases: enzymatic consequences of targeted alterations of the protein structure
    • Kühn H., Saam J., Eibach S., Holzhutter H.G., Ivanov I., and Walther M. Structural biology of mammalian lipoxygenases: enzymatic consequences of targeted alterations of the protein structure. Biochem. Biophys. Res. Commun. 338 (2005) 93-101
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 93-101
    • Kühn, H.1    Saam, J.2    Eibach, S.3    Holzhutter, H.G.4    Ivanov, I.5    Walther, M.6
  • 29
    • 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
    • Walther M., Wiesner R., and Kühn H. 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
    • (2004) J. Biol. Chem. , vol.279 , pp. 3717-3725
    • Walther, M.1    Wiesner, R.2    Kühn, H.3
  • 30
    • 0032480811 scopus 로고    scopus 로고
    • Uncovering a calcium-regulated membrane-binding mechanism for soybean lipoxygenase-1
    • Tatulian S.A., Steczko J., and Minor W. Uncovering a calcium-regulated membrane-binding mechanism for soybean lipoxygenase-1. Biochemistry 37 (1998) 15481-15490
    • (1998) Biochemistry , vol.37 , pp. 15481-15490
    • Tatulian, S.A.1    Steczko, J.2    Minor, W.3
  • 31
    • 28244498659 scopus 로고    scopus 로고
    • Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via a C2-like domain and a structural basis of product chirality
    • Oldham M.L., Brash A.R., and Newcomer M.E. Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via a C2-like domain and a structural basis of product chirality. J. Biol. Chem. 280 (2005) 39545-39552
    • (2005) J. Biol. Chem. , vol.280 , pp. 39545-39552
    • Oldham, M.L.1    Brash, A.R.2    Newcomer, M.E.3
  • 32
    • 18144375533 scopus 로고    scopus 로고
    • Structural stability of soybean lipoxygenase-1 in solution as probed by small angle X-ray scattering
    • Dainese E., Sabatucci A., van Zadelhoff G., Angelucci C.B., Vachette P., Veldink G.A., et al. Structural stability of soybean lipoxygenase-1 in solution as probed by small angle X-ray scattering. J. Mol. Biol. 349 (2005) 143-152
    • (2005) J. Mol. Biol. , vol.349 , pp. 143-152
    • Dainese, E.1    Sabatucci, A.2    van Zadelhoff, G.3    Angelucci, C.B.4    Vachette, P.5    Veldink, G.A.6
  • 33
    • 5144223918 scopus 로고    scopus 로고
    • 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
    • Hammel M., Walther M., Prassl R., and Kühn H. 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
    • (2004) J. Mol. Biol. , vol.343 , pp. 917-929
    • Hammel, M.1    Walther, M.2    Prassl, R.3    Kühn, H.4
  • 34
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • Painter J., and Merrit E.A. TLSMD web server for the generation of multi-group TLS models. J. Appl. Cryst. 39 (2006) 109-111
    • (2006) J. Appl. Cryst. , vol.39 , pp. 109-111
    • Painter, J.1    Merrit, E.A.2
  • 35
    • 33745635868 scopus 로고    scopus 로고
    • Effect of crystal freezing and small-molecule binding on internal cavity size in a large protein: X-ray and docking studies of lipoxygenase at ambient and low temperature at 2.0 A resolution
    • Skrzypczak-Jankun E., Borbulevych O.Y., Zavodszky M.I., Baranski M.R., Padmanabhan K., Petricek V., and Jankun J. Effect of crystal freezing and small-molecule binding on internal cavity size in a large protein: X-ray and docking studies of lipoxygenase at ambient and low temperature at 2.0 A resolution. Acta Crystallogr., Sect. D: Biol. Crystallogr. 62 (2006) 766-775
    • (2006) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.62 , pp. 766-775
    • Skrzypczak-Jankun, E.1    Borbulevych, O.Y.2    Zavodszky, M.I.3    Baranski, M.R.4    Padmanabhan, K.5    Petricek, V.6    Jankun, J.7
  • 37
    • 0031460029 scopus 로고    scopus 로고
    • PDZ domain proteins: scaffolds for signaling complexes
    • Ranganathan R., and Ross E.M. PDZ domain proteins: scaffolds for signaling complexes. Curr. Biol. 7 (1997) R770-R773
    • (1997) Curr. Biol. , vol.7
    • Ranganathan, R.1    Ross, E.M.2
  • 39
    • 0033560065 scopus 로고    scopus 로고
    • PDZ domains: fundamental building blocks in the organization of protein complexes at the plasma membrane
    • Fanning A.S., and Anderson J.M. PDZ domains: fundamental building blocks in the organization of protein complexes at the plasma membrane. J. Clin. Invest. 103 (1999) 767-772
    • (1999) J. Clin. Invest. , vol.103 , pp. 767-772
    • Fanning, A.S.1    Anderson, J.M.2
  • 40
    • 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., et al. Exploring sponge-derived terpenoids for their potency and selectivity against 12-human, 15-human, and 15-soybean lipoxygenases. J. Nat. Prod. 66 (2003) 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
  • 42
    • 77957001732 scopus 로고
    • Reaction of protein sulfhydryl groups with Ellman's reagent
    • Habeeb A.S.A. Reaction of protein sulfhydryl groups with Ellman's reagent. Methods Enzymol. 25 (1972) 457-464
    • (1972) Methods Enzymol. , vol.25 , pp. 457-464
    • Habeeb, A.S.A.1
  • 44
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31 (2003) 3381-3385
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 45
    • 0036283048 scopus 로고    scopus 로고
    • Evolution and physics in comparative protein structure modeling
    • Fiser A., Feig M., Brooks III C.L., and Sali A. Evolution and physics in comparative protein structure modeling. Acc. Chem. Res. 35 (2002) 413-421
    • (2002) Acc. Chem. Res. , vol.35 , pp. 413-421
    • Fiser, A.1    Feig, M.2    Brooks III, C.L.3    Sali, A.4
  • 46
    • 0000082544 scopus 로고
    • CHAIN-a crystallographic modeling program
    • Sack J.S. CHAIN-a crystallographic modeling program. J. Mol. Graphics 6 (1988) 224-225
    • (1988) J. Mol. Graphics , vol.6 , pp. 224-225
    • Sack, J.S.1
  • 47
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., McArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26 (1993) 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 48
    • 38049141046 scopus 로고    scopus 로고
    • DeLano, W. L. (2005). The PyMOL molecular graphics system. PyMOL v.0.98. DeLano Scientific, Palo Alto, CA.
  • 49
    • 0001498978 scopus 로고
    • La diffraction des rayons X aux tres petits angles; application a l'etude de phenomenes ultramicroscopiques
    • Guinier A. La diffraction des rayons X aux tres petits angles; application a l'etude de phenomenes ultramicroscopiques. Ann. Phys. (Paris) 12 (1939) 161-237
    • (1939) Ann. Phys. (Paris) , vol.12 , pp. 161-237
    • Guinier, A.1
  • 50
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect transform methods using perceptual criteria
    • Svergun D.I. Determination of the regularization parameter in indirect transform methods using perceptual criteria. J. Appl. Crystallogr. 25 (1992) 495-503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 51
    • 0002720864 scopus 로고
    • General theory
    • Glatter O., and Kratky O. (Eds), Academic Press, London
    • Porod G. General theory. In: Glatter O., and Kratky O. (Eds). Small-angle X-ray scattering (1982), Academic Press, London 17-51
    • (1982) Small-angle X-ray scattering , pp. 17-51
    • Porod, G.1
  • 52
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin M.B., and Svergun D.I. Automated matching of high- and low-resolution structural models. J. Appl. Crystallogr. 34 (2001) 33-41
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 53
    • 0029185933 scopus 로고
    • CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D.I., Barberato C., and Koch M.H.J. CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28 (1995) 768-773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3


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