메뉴 건너뛰기




Volumn 22, Issue 10, 2013, Pages 1432-1438

Crystal structures of α-dioxygenase from Oryza sativa: Insights into substrate binding and activation by hydrogen peroxide

Author keywords

dioxygenase; Cyclooxygenase; Fatty acids; Oxylipins; X ray crystallography

Indexed keywords

ALPHA DIOXYGENASE; ARGININE; ASPARAGINE; DIOXYGENASE; HISTONE; HYDROGEN PEROXIDE; PALMITIC ACID; THREONINE; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 84892917687     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2327     Document Type: Article
Times cited : (12)

References (28)
  • 1
    • 0036633804 scopus 로고    scopus 로고
    • Impact of phyto-Oxylipins in plant defense
    • Blee E (2002) Impact of phyto-Oxylipins in plant defense. Trends Plant Sci 7:315-322.
    • (2002) Trends Plant Sci , vol.7 , pp. 315-322
    • Blee, E.1
  • 2
    • 0030266346 scopus 로고    scopus 로고
    • Resistance gene-Dependent plant defense responses
    • Hammond-Kosack KE, Jones JD (1996) Resistance gene-Dependent plant defense responses. Plant Cell 8: 1773-1791.
    • (1996) Plant Cell , vol.8 , pp. 1773-1791
    • Hammond-Kosack, K.E.1    Jones, J.D.2
  • 3
    • 0032171144 scopus 로고    scopus 로고
    • PIOX, a new pathogen-Induced oxygenase with homology to animal cyclooxygenase
    • Sanz A, Moreno JI, Castresana C (1998) PIOX, a new pathogen-Induced oxygenase with homology to animal cyclooxygenase. Plant Cell 10:1523-1537.
    • (1998) Plant Cell , vol.10 , pp. 1523-1537
    • Sanz, A.1    Moreno, J.I.2    Castresana, C.3
  • 4
    • 46449130668 scopus 로고    scopus 로고
    • The peroxidase-Cyclooxygenase superfamily: Reconstructed evolution of critical enzymes of the innate immune system
    • Zamocky M, Jakopitsch C, Furtmuller PG, Dunand C, Obinger C (2008) The peroxidase-Cyclooxygenase superfamily: Reconstructed evolution of critical enzymes of the innate immune system. Proteins 72:589-605.
    • (2008) Proteins , vol.72 , pp. 589-605
    • Zamocky, M.1    Jakopitsch, C.2    Furtmuller, P.G.3    Dunand, C.4    Obinger, C.5
  • 5
    • 84874413608 scopus 로고    scopus 로고
    • The crystal structure of alpha-Dioxygenase provides insight into diversity in the cyclooxygenaseperoxidase superfamily
    • Goulah CC, Zhu G, Koszelak-Rosenblum M, Malkowski MG (2013) The crystal structure of alpha-Dioxygenase provides insight into diversity in the cyclooxygenaseperoxidase superfamily. Biochemistry 52:1364-1372.
    • (2013) Biochemistry , vol.52 , pp. 1364-1372
    • Goulah, C.C.1    Zhu, G.2    Koszelak-Rosenblum, M.3    Malkowski, M.G.4
  • 8
    • 0033609815 scopus 로고    scopus 로고
    • Alpha-Oxidation of fatty acids in higher plants
    • Hamberg M, Sanz A, Casresana C (1999) Alpha-Oxidation of fatty acids in higher plants. J Biol Chem 274: 24503-24513.
    • (1999) J Biol Chem , vol.274 , pp. 24503-24513
    • Hamberg, M.1    Sanz, A.2    Casresana, C.3
  • 9
    • 78651393044 scopus 로고    scopus 로고
    • Catalytic mechanism of a heme and tyrosyl radical-Containing fatty acid alpha-(di)oxygenase
    • Mukherjee A, Angeles-Boza AM, Huff GS, Roth JP (2011) Catalytic mechanism of a heme and tyrosyl radical-Containing fatty acid alpha-(di)oxygenase. J Am Chem Soc 133:227-238.
    • (2011) J Am Chem Soc , vol.133 , pp. 227-238
    • Mukherjee, A.1    Angeles-Boza, A.M.2    Huff, G.S.3    Roth, J.P.4
  • 10
    • 34248596797 scopus 로고    scopus 로고
    • Control of oxygenation in lipoxygenase and cyclooxygenase catalysis
    • Schneider C, Pratt DA, Porter NA, Brash AR (2007) Control of oxygenation in lipoxygenase and cyclooxygenase catalysis. Chem Biol 14:473-488.
    • (2007) Chem Biol , vol.14 , pp. 473-488
    • Schneider, C.1    Pratt, D.A.2    Porter, N.A.3    Brash, A.R.4
  • 11
    • 0034665857 scopus 로고    scopus 로고
    • The productive conformation of arachidonic acid bound to prostaglandin synthase
    • Malkowski MG, Ginell SL, Smith WL, Garavito RM (2000) The productive conformation of arachidonic acid bound to prostaglandin synthase. Science 289:1933-1937.
    • (2000) Science , vol.289 , pp. 1933-1937
    • Malkowski, M.G.1    Ginell, S.L.2    Smith, W.L.3    Garavito, R.M.4
  • 12
    • 77954611060 scopus 로고    scopus 로고
    • Structural basis of fatty acid substrate binding to cyclooxygenase-2
    • Vecchio AJ, Simmons DM, Malkowski MG (2010) Structural basis of fatty acid substrate binding to cyclooxygenase-2. J Biol Chem 285:22152-22163.
    • (2010) J Biol Chem , vol.285 , pp. 22152-22163
    • Vecchio, A.J.1    Simmons, D.M.2    Malkowski, M.G.3
  • 13
  • 15
    • 3142766245 scopus 로고    scopus 로고
    • Characterization of the heme environment in Arabidopsis thaliana fatty acid alpha-Dioxygenase
    • Liu W, Rogge CE, Bambai B, Palmer G, Tsai AL, Kulmacz RJ (2004) Characterization of the heme environment in Arabidopsis thaliana fatty acid alpha-Dioxygenase-J Biol Chem 279:29805-29815.
    • (2004) J Biol Chem , vol.279 , pp. 29805-29815
    • Liu, W.1    Rogge, C.E.2    Bambai, B.3    Palmer, G.4    Tsai, A.L.5    Kulmacz, R.J.6
  • 18
    • 79955442040 scopus 로고    scopus 로고
    • Lessons from high-Throughput protein crystallization screening: 10 years of practical experience
    • Luft JR, Snell EH, DeTitta GT (2011) Lessons from high-Throughput protein crystallization screening: 10 years of practical experience. Expert Opin Drug Discov 6:465-480.
    • (2011) Expert Opin Drug Discov , vol.6 , pp. 465-480
    • Luft, J.R.1    Snell, E.H.2    Detitta, G.T.3
  • 19
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-Ray diffraction data collected in oscillation mode
    • In Carter, Jr CW, Sweet RM, Eds. New York Academic Press
    • Otwinowski Z, Minor W, Processing of X-Ray diffraction data collected in oscillation mode. In Carter, Jr CW, Sweet RM, Eds. (1997) Methods in enzymology. New York: Academic Press, pp 307-326.
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 22
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-Ray crystallography using ARP/wARP version
    • Langer G, Cohen SX, Lamzin VS, Perrakis A (2008) Automated macromolecular model building for X-Ray crystallography using ARP/wARP version. Nat Protoc 3:1171-1179.
    • (2008) Nat Protoc , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 23
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-Building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-Building tools for molecular graphics. Acta Cryst D 60:2126-2132.
    • (2004) Acta Cryst D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 24
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximumlikelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximumlikelihood method. Acta Cryst D 53:240-255.
    • (1997) Acta Cryst D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 25
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotrophic displacements in macromolecular refinement
    • Winn MC, Isupov MN, Murshudov G (2000) Use of TLS parameters to model anisotrophic displacements in macromolecular refinement. Acta Cryst D 57:122-133.
    • (2000) Acta Cryst D , vol.57 , pp. 122-133
    • Winn, M.C.1    Isupov, M.N.2    Murshudov, G.3
  • 26
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P (2006) Scaling and assessment of data quality. Acta Cryst D 62:72-82.
    • (2006) Acta Cryst D , vol.62 , pp. 72-82
    • Evans, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.