메뉴 건너뛰기




Volumn 53, Issue 31, 2014, Pages 5102-5110

Fluctuations of an exposed π-helix involved in lipoxygenase substrate recognition

Author keywords

[No Author keywords available]

Indexed keywords

DYNAMICS; IRON; MAGNETIC RESONANCE; SUBSTRATES;

EID: 84905995133     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500768c     Document Type: Article
Times cited : (16)

References (44)
  • 1
    • 77955495763 scopus 로고    scopus 로고
    • Location, location, location: Compartmentalization of early events in leukotriene biosynthesis
    • Newcomer, M. E. and Gilbert, N. C. (2010) Location, location, location: Compartmentalization of early events in leukotriene biosynthesis J. Biol. Chem. 285, 25109-25114
    • (2010) J. Biol. Chem. , vol.285 , pp. 25109-25114
    • Newcomer, M.E.1    Gilbert, N.C.2
  • 2
    • 79955670124 scopus 로고    scopus 로고
    • Resolvins and protectins in inflammation resolution
    • Serhan, C. N. and Petasis, N. A. (2011) Resolvins and protectins in inflammation resolution Chem. Rev. 111, 5922-5943
    • (2011) Chem. Rev. , vol.111 , pp. 5922-5943
    • Serhan, C.N.1    Petasis, N.A.2
  • 3
    • 30944470221 scopus 로고    scopus 로고
    • Lipoxygenases: Occurrence, functions and catalysis
    • Liavonchanka, A. and Feussner, N. (2006) Lipoxygenases: Occurrence, functions and catalysis J. Plant Physiol. 163, 348-357
    • (2006) J. Plant Physiol. , vol.163 , pp. 348-357
    • Liavonchanka, A.1    Feussner, N.2
  • 5
    • 84864742277 scopus 로고    scopus 로고
    • Conversion of human 5-lipoxygenase to a 15-lipoxygenase by a point mutation to mimic phosphorylation at serine-663
    • Gilbert, N. C., Rui, Z., Neau, D. B., Waight, M. T., Bartlett, S. G., Boeglin, W. E., Brash, A. R., and Newcomer, M. E. (2012) Conversion of human 5-lipoxygenase to a 15-lipoxygenase by a point mutation to mimic phosphorylation at serine-663 FASEB J. 26, 3222-3229
    • (2012) FASEB J. , vol.26 , pp. 3222-3229
    • Gilbert, N.C.1    Rui, Z.2    Neau, D.B.3    Waight, M.T.4    Bartlett, S.G.5    Boeglin, W.E.6    Brash, A.R.7    Newcomer, M.E.8
  • 7
  • 8
    • 0029922801 scopus 로고    scopus 로고
    • Lipoxygenases: Structural Principles and Spectroscopy
    • In (Stroud, R. M. Ed.) pp, Annual Reviews, Palo Alto, CA.
    • Gaffney, B. J. (1996) Lipoxygenases: Structural Principles and Spectroscopy. In Annual Reviews of Biophysics and Biomolecular Structure (Stroud, R. M., Ed.) pp 431-459, Annual Reviews, Palo Alto, CA.
    • (1996) Annual Reviews of Biophysics and Biomolecular Structure , pp. 431-459
    • Gaffney, B.J.1
  • 9
    • 0037769716 scopus 로고    scopus 로고
    • Manganese lipoxygenase has a mononuclear redox center
    • Su, C., Sahlin, M., and Oliw, E. H. (2002) Manganese lipoxygenase has a mononuclear redox center Adv. Exp. Med. Biol. 507, 171-176
    • (2002) Adv. Exp. Med. Biol. , vol.507 , pp. 171-176
    • Su, C.1    Sahlin, M.2    Oliw, E.H.3
  • 10
    • 84902239807 scopus 로고    scopus 로고
    • Extremely elevated room-temperature kinetic isotope effects quantify the critical role of barrier width in enzymatic C-H activation
    • Hu, S., Sharma, S. C., Scouras, A. D., Soudackov, A. V., Carr, C. A., Hammes-Schiffer, S., Alber, T., and Klinman, J. P. (2014) Extremely elevated room-temperature kinetic isotope effects quantify the critical role of barrier width in enzymatic C-H activation J. Am. Chem. Soc. 136, 8157-8160
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 8157-8160
    • Hu, S.1    Sharma, S.C.2    Scouras, A.D.3    Soudackov, A.V.4    Carr, C.A.5    Hammes-Schiffer, S.6    Alber, T.7    Klinman, J.P.8
  • 11
    • 84898839850 scopus 로고    scopus 로고
    • Hydrogen Tunneling in a Prokaryotic Lipoxygenase
    • Carr, C. A. M. and Klinman, J. P. (2014) Hydrogen Tunneling in a Prokaryotic Lipoxygenase Biochemistry 53, 2212-2214
    • (2014) Biochemistry , vol.53 , pp. 2212-2214
    • Carr, C.A.M.1    Klinman, J.P.2
  • 12
    • 84878830962 scopus 로고    scopus 로고
    • Gaining insight into the chemistry of lipoxygenases: A computational investigation into the catalytic mechanism of (8R)-lipoxygenase
    • Bushnell, E. A. C., Jamil, R., and Gauld, J. W. (2013) Gaining insight into the chemistry of lipoxygenases: A computational investigation into the catalytic mechanism of (8R)-lipoxygenase JBIC, J. Biol. Inorg. Chem. 18, 343-355
    • (2013) JBIC, J. Biol. Inorg. Chem. , vol.18 , pp. 343-355
    • Bushnell, E.A.C.1    Jamil, R.2    Gauld, J.W.3
  • 13
    • 0024562115 scopus 로고
    • Soybean lipoxygenase-1 enzymically forms both (9S)- and (13S)-hydroperoxides from linoleic acid by a pH-dependent mechanism
    • Gardner, H. W. (1989) Soybean lipoxygenase-1 enzymically forms both (9S)- and (13S)-hydroperoxides from linoleic acid by a pH-dependent mechanism Biochim. Biophys. Acta 1001, 274-281
    • (1989) Biochim. Biophys. Acta , vol.1001 , pp. 274-281
    • Gardner, H.W.1
  • 14
    • 84872964202 scopus 로고    scopus 로고
    • Conversion of pro-inflammatory murine Alox5 into an anti-inflammatory 15S-lipoxygenating enzyme by multiple mutations of sequence determinants
    • Hofheinz, K., Kakularam, K. R., Adel, S., Anton, M., Polymarasetty, A., Reddanna, P., Kuhn, H., and Horn, T. (2013) Conversion of pro-inflammatory murine Alox5 into an anti-inflammatory 15S-lipoxygenating enzyme by multiple mutations of sequence determinants Arch. Biochem. Biophys. 530, 40-47
    • (2013) Arch. Biochem. Biophys. , vol.530 , pp. 40-47
    • Hofheinz, K.1    Kakularam, K.R.2    Adel, S.3    Anton, M.4    Polymarasetty, A.5    Reddanna, P.6    Kuhn, H.7    Horn, T.8
  • 15
    • 38549129314 scopus 로고    scopus 로고
    • Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data
    • Choi, J., Chon, J. K., Kim, S., and Shin, W. (2008) Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data Proteins 70, 1023-1032
    • (2008) Proteins , vol.70 , pp. 1023-1032
    • Choi, J.1    Chon, J.K.2    Kim, S.3    Shin, W.4
  • 16
    • 84865800398 scopus 로고    scopus 로고
    • Crystal Structure of 12-Lipoxygenase Catalytic-Domain-Inhibitor Complex Identifies a Substrate-Binding Channel for Catalysis
    • Xu, S., Mueser, T. C., Marnett, L. J., and Funk, M. O. (2012) Crystal Structure of 12-Lipoxygenase Catalytic-Domain-Inhibitor Complex Identifies a Substrate-Binding Channel for Catalysis Structure 20, 1490-1497
    • (2012) Structure , vol.20 , pp. 1490-1497
    • Xu, S.1    Mueser, T.C.2    Marnett, L.J.3    Funk, M.O.4
  • 17
    • 0027246677 scopus 로고
    • The 3-Dimensional Structure of an Arachidonic-Acid 15-Lipoxygenase
    • Boyington, J. C., Gaffney, B. J., and Amzel, L. M. (1993) The 3-Dimensional Structure of an Arachidonic-Acid 15-Lipoxygenase Science 260, 1482-1486
    • (1993) Science , vol.260 , pp. 1482-1486
    • Boyington, J.C.1    Gaffney, B.J.2    Amzel, L.M.3
  • 19
    • 33751099583 scopus 로고    scopus 로고
    • Crystal structures of vegetative soybean lipoxygenase VLX-B and VLX-D, and comparisons with seed isoforms LOX-1 and LOX-3
    • Youn, B., Sellhorn, G. E., Mirchel, R. J., Gaffney, B. J., Grimes, H. D., and Kang, C. (2006) Crystal structures of vegetative soybean lipoxygenase VLX-B and VLX-D, and comparisons with seed isoforms LOX-1 and LOX-3 Proteins 65, 1008-1020
    • (2006) Proteins , vol.65 , pp. 1008-1020
    • Youn, B.1    Sellhorn, G.E.2    Mirchel, R.J.3    Gaffney, B.J.4    Grimes, H.D.5    Kang, C.6
  • 20
    • 0030930205 scopus 로고    scopus 로고
    • Structure of soybean lipoxygenase L3 and a comparison with its L1 isoenzyme
    • Skrzypczak-Jankun, E., Amzel, L. M., Kroa, B. A., and Funk, M. O., Jr. (1997) Structure of soybean lipoxygenase L3 and a comparison with its L1 isoenzyme Proteins 29, 15-31
    • (1997) Proteins , vol.29 , pp. 15-31
    • Skrzypczak-Jankun, E.1    Amzel, L.M.2    Kroa, B.A.3    Funk Jr., M.O.4
  • 21
    • 33644669435 scopus 로고    scopus 로고
    • On the relationships of substrate orientation, hydrogen abstraction, and product stereochemistry in single and double dioxygenations by soybean lipoxygenase-1 and its Ala542Gly mutant
    • Coffa, G., Imber, A. N., Maguire, B. C., Laxmikanthan, G., Schneider, C., Gaffney, B. J., and Brash, A. R. (2005) On the relationships of substrate orientation, hydrogen abstraction, and product stereochemistry in single and double dioxygenations by soybean lipoxygenase-1 and its Ala542Gly mutant J. Biol. Chem. 280, 38756-38766
    • (2005) J. Biol. Chem. , vol.280 , pp. 38756-38766
    • Coffa, G.1    Imber, A.N.2    Maguire, B.C.3    Laxmikanthan, G.4    Schneider, C.5    Gaffney, B.J.6    Brash, A.R.7
  • 22
    • 0141706648 scopus 로고    scopus 로고
    • Kinetic studies of oxygen reactivity in soybean lipoxygenase-1
    • Knapp, M. J. and Klinman, J. P. (2003) Kinetic studies of oxygen reactivity in soybean lipoxygenase-1 Biochemistry 42, 11466-11475
    • (2003) Biochemistry , vol.42 , pp. 11466-11475
    • Knapp, M.J.1    Klinman, J.P.2
  • 24
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • Stoll, S. and Schweiger, A. (2006) EasySpin, a comprehensive software package for spectral simulation and analysis in EPR J. Magn. Reson. 178, 42-55
    • (2006) J. Magn. Reson. , vol.178 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2
  • 25
    • 0027299131 scopus 로고
    • Using Nitroxide Spin Labels: How to Obtain T(1e) from Continuous Wave Electron-Paramagnetic Resonance-Spectra at All Rotational Rates
    • Haas, D. A., Mailer, C., and Robinson, B. H. (1993) Using Nitroxide Spin Labels: How to Obtain T(1e) from Continuous Wave Electron-Paramagnetic Resonance-Spectra at All Rotational Rates Biophys. J. 64, 594-604
    • (1993) Biophys. J. , vol.64 , pp. 594-604
    • Haas, D.A.1    Mailer, C.2    Robinson, B.H.3
  • 26
    • 0028346566 scopus 로고
    • A Collision Gradient-Method to Determine the Immersion Depth of Nitroxides in Lipid Bilayers: Application to Spin-Labeled Mutants of Bacteriorhodopsin
    • Altenbach, C., Greenhalgh, D. A., Khorana, H. G., and Hubbell, W. L. (1994) A Collision Gradient-Method to Determine the Immersion Depth of Nitroxides in Lipid Bilayers: Application to Spin-Labeled Mutants of Bacteriorhodopsin Proc. Natl. Acad. Sci. U.S.A. 91, 1667-1671
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1667-1671
    • Altenbach, C.1    Greenhalgh, D.A.2    Khorana, H.G.3    Hubbell, W.L.4
  • 27
    • 0032560604 scopus 로고    scopus 로고
    • Ligand-induced conformational change in the ferric enterobactin receptor FepA as studied by site-directed spin labeling and time-domain ESR
    • Klug, C. S., Eaton, S. S., Eaton, G. R., and Feix, J. B. (1998) Ligand-induced conformational change in the ferric enterobactin receptor FepA as studied by site-directed spin labeling and time-domain ESR Biochemistry 37, 9016-9023
    • (1998) Biochemistry , vol.37 , pp. 9016-9023
    • Klug, C.S.1    Eaton, S.S.2    Eaton, G.R.3    Feix, J.B.4
  • 28
    • 0026580066 scopus 로고
    • Using Saturation Recovery EPR to Measure Distances in Proteins: Applications to Photosystem-II
    • Hirsh, D. J., Beck, W. F., Innes, J. B., and Brudvig, G. W. (1992) Using Saturation Recovery EPR to Measure Distances in Proteins: Applications to Photosystem-II Biochemistry 31, 532-541
    • (1992) Biochemistry , vol.31 , pp. 532-541
    • Hirsh, D.J.1    Beck, W.F.2    Innes, J.B.3    Brudvig, G.W.4
  • 29
    • 0001752117 scopus 로고    scopus 로고
    • Electron Paramagnetic Resonance Distance Measurements in Photosynthetic Reaction Centers
    • In (Berliner, L. W. Eaton, S. S. and Eaton, G. R. Eds.) Kluwer, New York.
    • Lakshmi, K. V. and Brudvig, G. W. (2000) Electron Paramagnetic Resonance Distance Measurements in Photosynthetic Reaction Centers. In Distance Measurements in Biological Systems by EPR (Berliner, L. W., Eaton, S. S., and Eaton, G. R., Eds.) Kluwer, New York.
    • (2000) Distance Measurements in Biological Systems by EPR
    • Lakshmi, K.V.1    Brudvig, G.W.2
  • 30
    • 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 angstrom resolution
    • Skrzypczak-Jankun, E., Borbulevych, O. Y., Zavodszky, M. I., Baranski, M. R., Padmanabhan, K., Petricek, V., and Jankun, J. (2006) 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 angstrom resolution Acta Crystallogr D 62, 766-775
    • (2006) Acta Crystallogr D , 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
  • 31
    • 0039171268 scopus 로고    scopus 로고
    • Crystal structures of spin labeled T4 lysozyme mutants: Implications for the interpretation of EPR spectra in terms of structure
    • Langen, R., Oh, K. J., Cascio, D., and Hubbell, W. L. (2000) Crystal structures of spin labeled T4 lysozyme mutants: Implications for the interpretation of EPR spectra in terms of structure Biochemistry 39, 8396-8405
    • (2000) Biochemistry , vol.39 , pp. 8396-8405
    • Langen, R.1    Oh, K.J.2    Cascio, D.3    Hubbell, W.L.4
  • 33
    • 0038245156 scopus 로고    scopus 로고
    • The role of α-, 3(10)-, and π-helix in helix → coil transitions
    • Armen, R., Alonso, D. O. V., and Daggett, V. (2003) The role of α-, 3(10)-, and π-helix in helix → coil transitions Protein Sci. 12, 1145-1157
    • (2003) Protein Sci. , vol.12 , pp. 1145-1157
    • Armen, R.1    Alonso, D.O.V.2    Daggett, V.3
  • 34
    • 78349305451 scopus 로고    scopus 로고
    • Evolutionary origin of a secondary structure: π-Helices as cryptic but widespread insertional variations of α-helices that enhance protein functionality
    • Cooley, R. B., Arp, D. J., and Karplus, P. A. (2010) Evolutionary origin of a secondary structure: π-Helices as cryptic but widespread insertional variations of α-helices that enhance protein functionality J. Mol. Biol. 404, 232-246
    • (2010) J. Mol. Biol. , vol.404 , pp. 232-246
    • Cooley, R.B.1    Arp, D.J.2    Karplus, P.A.3
  • 35
    • 0027467033 scopus 로고
    • The α-Aneurysm: A Structural Motif Revealed in an Insertion Mutant of Staphylococcal Nuclease
    • Keefe, L. J., Sondek, J., Shortle, D., and Lattman, E. E. (1993) The α-Aneurysm: A Structural Motif Revealed in an Insertion Mutant of Staphylococcal Nuclease Proc. Natl. Acad. Sci. U.S.A. 90, 3275-3279
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 3275-3279
    • Keefe, L.J.1    Sondek, J.2    Shortle, D.3    Lattman, E.E.4
  • 36
    • 33750692730 scopus 로고    scopus 로고
    • Linoleoyl lysophosphatidylcholine is an efficient substrate for soybean lipoxygenase-1
    • Huang, L. S., Kim, M. R., and Sok, D. E. (2006) Linoleoyl lysophosphatidylcholine is an efficient substrate for soybean lipoxygenase-1 Arch. Biochem. Biophys. 455, 119-126
    • (2006) Arch. Biochem. Biophys. , vol.455 , pp. 119-126
    • Huang, L.S.1    Kim, M.R.2    Sok, D.E.3
  • 37
    • 0037059138 scopus 로고    scopus 로고
    • Molecular orbital study of polarity and hydrogen bonding effects on the g and hyperfine tensors of site directed NO spin labelled bacteriorhodopsin
    • Plato, M., Steinhoff, H. J., Wegener, C., Torring, J. T., Savitsky, A., and Mobius, K. (2002) Molecular orbital study of polarity and hydrogen bonding effects on the g and hyperfine tensors of site directed NO spin labelled bacteriorhodopsin Mol. Phys. 100, 3711-3721
    • (2002) Mol. Phys. , vol.100 , pp. 3711-3721
    • Plato, M.1    Steinhoff, H.J.2    Wegener, C.3    Torring, J.T.4    Savitsky, A.5    Mobius, K.6
  • 39
    • 0020997912 scopus 로고
    • Dictionary of Protein Secondary Structure: Pattern-Recognition of Hydrogen-Bonded and Geometrical Features
    • Kabsch, W. and Sander, C. (1983) Dictionary of Protein Secondary Structure: Pattern-Recognition of Hydrogen-Bonded and Geometrical Features Biopolymers 22, 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 40
    • 0033155811 scopus 로고    scopus 로고
    • Electron spin lattice relaxation rates for S=1/2 molecular species in glassy matrices or magnetically dilute solids at temperatures between 10 and 300 K
    • Zhou, Y., Bowler, B. E., Eaton, G. R., and Eaton, S. S. (1999) Electron spin lattice relaxation rates for S=1/2 molecular species in glassy matrices or magnetically dilute solids at temperatures between 10 and 300 K J. Magn. Reson. 139, 165-174
    • (1999) J. Magn. Reson. , vol.139 , pp. 165-174
    • Zhou, Y.1    Bowler, B.E.2    Eaton, G.R.3    Eaton, S.S.4
  • 42
    • 33751385929 scopus 로고
    • Long-Range Electron-Spin Spin Interactions in the Bacterial Photosynthetic Reaction-Center
    • Hirsh, D. J. and Brudvig, G. W. (1993) Long-Range Electron-Spin Spin Interactions in the Bacterial Photosynthetic Reaction-Center J. Phys. Chem. 97, 13216-13222
    • (1993) J. Phys. Chem. , vol.97 , pp. 13216-13222
    • Hirsh, D.J.1    Brudvig, G.W.2
  • 43
    • 0028992420 scopus 로고
    • Near-Infrared Circular-Dichroism, Magnetic Circular-Dichroism, and X-ray-Absorption Spectral Comparison of the Nonheme Ferrous Active-Sites of Plant and Mammalian 15-Lipoxygenases
    • Pavlosky, M. A., Zhang, Y., Westre, T. E., Gan, Q. F., Pavel, E. G., Campochiaro, C., Hedman, B., Hodgson, K. O., and Solomon, E. I. (1995) Near-Infrared Circular-Dichroism, Magnetic Circular-Dichroism, and X-ray-Absorption Spectral Comparison of the Nonheme Ferrous Active-Sites of Plant and Mammalian 15-Lipoxygenases J. Am. Chem. Soc. 117, 4316-4327
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 4316-4327
    • Pavlosky, M.A.1    Zhang, Y.2    Westre, T.E.3    Gan, Q.F.4    Pavel, E.G.5    Campochiaro, C.6    Hedman, B.7    Hodgson, K.O.8    Solomon, E.I.9
  • 44
    • 0036276409 scopus 로고    scopus 로고
    • Occurrence, conformational features and amino acid propensities for the π-helix
    • Fodje, M. N. and Al-Karadaghi, S. (2002) Occurrence, conformational features and amino acid propensities for the π-helix Protein Eng. 15, 353-358
    • (2002) Protein Eng. , vol.15 , pp. 353-358
    • Fodje, M.N.1    Al-Karadaghi, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.