메뉴 건너뛰기




Volumn 338, Issue 1, 2005, Pages 198-205

Structure of catechol 1,2-dioxygenase from Pseudomonas arvilla

Author keywords

Intradiol dioxygenase; Lipid binding protein; Metalloenzyme; Nonheme iron; X ray crystallography

Indexed keywords

BACTERIAL ENZYME; CATECHOL 1,2 DIOXYGENASE; ISOENZYME; LIPID BINDING PROTEIN; POLYPEPTIDE;

EID: 27544468840     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.221     Document Type: Article
Times cited : (36)

References (37)
  • 1
    • 0002754238 scopus 로고
    • Pyrocatechase. a new enzyme catalyzing oxidative breakdown of pyrocatechin
    • O. Hayaishi, and K. Hashimoto Pyrocatechase. A new enzyme catalyzing oxidative breakdown of pyrocatechin J. Biochem. (Tokyo) 37 1950 371 374
    • (1950) J. Biochem. (Tokyo) , vol.37 , pp. 371-374
    • Hayaishi, O.1    Hashimoto, K.2
  • 4
    • 0034654852 scopus 로고    scopus 로고
    • The 1.8 Å crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker
    • M.W. Vetting, and D.H. Ohlendorf The 1.8 Å crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker Struct. Fold. Des. 8 2000 429 440
    • (2000) Struct. Fold. Des. , vol.8 , pp. 429-440
    • Vetting, M.W.1    Ohlendorf, D.H.2
  • 5
    • 0024296029 scopus 로고
    • Structure and assembly of protocatechuate 3,4-dioxygenase
    • D.H. Ohlendorf, J.D. Lipscomb, and P.C. Weber Structure and assembly of protocatechuate 3,4-dioxygenase Nature 336 1988 403 405
    • (1988) Nature , vol.336 , pp. 403-405
    • Ohlendorf, D.H.1    Lipscomb, J.D.2    Weber, P.C.3
  • 6
    • 20444401188 scopus 로고    scopus 로고
    • Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation
    • M. Ferraroni, J. Seifert, V.M. Travkin, M. Thiel, S. Kaschabek, A. Scozzafava, L. Golovleva, M. Schlomann, and F. Briganti Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation J. Biol. Chem. 280 2005 21144 21154
    • (2005) J. Biol. Chem. , vol.280 , pp. 21144-21154
    • Ferraroni, M.1    Seifert, J.2    Travkin, V.M.3    Thiel, M.4    Kaschabek, S.5    Scozzafava, A.6    Golovleva, L.7    Schlomann, M.8    Briganti, F.9
  • 7
    • 0021275478 scopus 로고
    • Brevibacterium fuscum protocatechuate 3,4-dioxygenase. Purification, crystallization, and characterization
    • J.W. Whittaker, J.D. Lipscomb, T.A. Kent, and E. Münck Brevibacterium fuscum protocatechuate 3,4-dioxygenase. Purification, crystallization, and characterization J. Biol. Chem. 259 1984 4466 4475
    • (1984) J. Biol. Chem. , vol.259 , pp. 4466-4475
    • Whittaker, J.W.1    Lipscomb, J.D.2    Kent, T.A.3    Münck, E.4
  • 9
    • 0030874393 scopus 로고    scopus 로고
    • Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase-multiple exogenous ligand binding orientations within the active site
    • A.M. Orville, N. Elango, J.D. Lipscomb, and D.H. Ohlendorf Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase-multiple exogenous ligand binding orientations within the active site Biochemistry 36 1997 10039 10051
    • (1997) Biochemistry , vol.36 , pp. 10039-10051
    • Orville, A.M.1    Elango, N.2    Lipscomb, J.D.3    Ohlendorf, D.H.4
  • 11
    • 0018390039 scopus 로고
    • Nonidentical subunits of pyrocatechase from Pseudomonas arvilla C-1
    • C. Nakai, H. Kagamiyama, Y. Saeki, and M. Nozaki Nonidentical subunits of pyrocatechase from Pseudomonas arvilla C-1 Arch. Biochem. Biophys. 195 1979 12 22
    • (1979) Arch. Biochem. Biophys. , vol.195 , pp. 12-22
    • Nakai, C.1    Kagamiyama, H.2    Saeki, Y.3    Nozaki, M.4
  • 12
    • 0025159432 scopus 로고
    • Three isozymes of catechol 1,2-dioxygenase (pyrocatechase), αα, αβ, and ββ, from Pseudomonas arvilla C-1
    • C. Nakai, K. Horiike, S. Kuramitsu, H. Kagamiyama, and M. Nozaki Three isozymes of catechol 1,2-dioxygenase (pyrocatechase), αα, αβ, and ββ, from Pseudomonas arvilla C-1 J. Biol. Chem. 265 1990 660 665
    • (1990) J. Biol. Chem. , vol.265 , pp. 660-665
    • Nakai, C.1    Horiike, K.2    Kuramitsu, S.3    Kagamiyama, H.4    Nozaki, M.5
  • 17
    • 0001897686 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • A.T. Brünger Free R value: a novel statistical quantity for assessing the accuracy of crystal structures Acta. Cryst. D 49 1992 24 46
    • (1992) Acta. Cryst. D , vol.49 , pp. 24-46
    • Brünger, A.T.1
  • 18
    • 0000356656 scopus 로고
    • A graphics model building program and refinement system for macromolecules
    • T.A. Jones A graphics model building program and refinement system for macromolecules J. Appl. Cryst. 11 1978 268 272
    • (1978) J. Appl. Cryst. , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 19
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • R.A. Laskowski, M.W. MacArthur, D.S. Moss, and J.M. Thornton PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Cryst. 26 1993 283 291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 20
    • 3042546949 scopus 로고    scopus 로고
    • Crystal structure of 4-chlorocatechol 1,2-dioxygenase from the chlorophenol-utilizing gram-positive Rhodococcus opacus 1CP
    • M. Ferraroni, I.P. Solyanikova, M.P. Kolomytseva, A. Scozzafava, L. Golovleva, and F. Briganti Crystal structure of 4-chlorocatechol 1,2-dioxygenase from the chlorophenol-utilizing gram-positive Rhodococcus opacus 1CP J. Biol. Chem. 279 2004 27646 27655
    • (2004) J. Biol. Chem. , vol.279 , pp. 27646-27655
    • Ferraroni, M.1    Solyanikova, I.P.2    Kolomytseva, M.P.3    Scozzafava, A.4    Golovleva, L.5    Briganti, F.6
  • 21
    • 0024356436 scopus 로고
    • Crystal structure of rat intestinal fatty-acid-binding protein. Refinement and analysis of the Escherichia coli-derived protein with bound palmitate
    • J.C. Sacchettini, J.I. Gordon, and L.J. Banaszak Crystal structure of rat intestinal fatty-acid-binding protein. Refinement and analysis of the Escherichia coli-derived protein with bound palmitate J. Mol. Biol. 208 1989 327 339
    • (1989) J. Mol. Biol. , vol.208 , pp. 327-339
    • Sacchettini, J.C.1    Gordon, J.I.2    Banaszak, L.J.3
  • 22
    • 0034684168 scopus 로고    scopus 로고
    • The lipocalin protein family: Structural and sequence overview
    • D.R. Flower, A.C. North, and C.E. Sansom The lipocalin protein family: structural and sequence overview Biochim. Biophys. Acta 1482 2000 9 24
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 9-24
    • Flower, D.R.1    North, A.C.2    Sansom, C.E.3
  • 24
    • 0033199578 scopus 로고    scopus 로고
    • The crystal structure of a wheat nonspecific lipid transfer protein (ns-LTP1) complexed with two molecules of phospholipid at 2.1 a resolution
    • D. Charvolin, J.P. Douliez, D. Marion, C. Cohen-Addad, and E. Pebay-Peyroula The crystal structure of a wheat nonspecific lipid transfer protein (ns-LTP1) complexed with two molecules of phospholipid at 2.1 A resolution Eur. J. Biochem. 264 1999 562 568
    • (1999) Eur. J. Biochem. , vol.264 , pp. 562-568
    • Charvolin, D.1    Douliez, J.P.2    Marion, D.3    Cohen-Addad, C.4    Pebay-Peyroula, E.5
  • 26
    • 17844377971 scopus 로고    scopus 로고
    • EPR studies of chlorocatechol 1,2-dioxygenase: Evidences of iron reduction during catalysis and of the binding of amphipatic molecules
    • A. Citadini, A. Pinto, A. Araujo, O. Nascimento, and A. Costa-Filho EPR studies of chlorocatechol 1,2-dioxygenase: evidences of iron reduction during catalysis and of the binding of amphipatic molecules Biophys. J. 88 2005 3502 3508
    • (2005) Biophys. J. , vol.88 , pp. 3502-3508
    • Citadini, A.1    Pinto, A.2    Araujo, A.3    Nascimento, O.4    Costa-Filho, A.5
  • 27
    • 0028067892 scopus 로고
    • Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 Å resolution
    • D.H. Ohlendorf, A.M. Orville, and J.D. Lipscomb Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 Å resolution J. Mol. Biol. 244 1994 586 608
    • (1994) J. Mol. Biol. , vol.244 , pp. 586-608
    • Ohlendorf, D.H.1    Orville, A.M.2    Lipscomb, J.D.3
  • 28
    • 0029780731 scopus 로고    scopus 로고
    • Amino acid sequence of catechol 1,2-dioxygenase (pyrocatechase) isozyme αα from Pseudomonas arvilla C-1
    • C. Nakai, G. Yamazaki, H. Kagamiyama, and M. Nozaki Amino acid sequence of catechol 1,2-dioxygenase (pyrocatechase) isozyme αα from Pseudomonas arvilla C-1 Biochem. Mol. Biol. Int. 39 1996 781 788
    • (1996) Biochem. Mol. Biol. Int. , vol.39 , pp. 781-788
    • Nakai, C.1    Yamazaki, G.2    Kagamiyama, H.3    Nozaki, M.4
  • 29
    • 0000093758 scopus 로고    scopus 로고
    • Functional models for catechol 1,2-dioxygenase-synthesis, structure, spectra, and catalytic activity of certain tripodal iron(III) complexes
    • R. Viswanathan, M. Palaniandavar, T. Balasubramanian, and T.P. Muthiah Functional models for catechol 1,2-dioxygenase-synthesis, structure, spectra, and catalytic activity of certain tripodal iron(III) complexes Inorg. Chem. 37 1998 2943 2951
    • (1998) Inorg. Chem. , vol.37 , pp. 2943-2951
    • Viswanathan, R.1    Palaniandavar, M.2    Balasubramanian, T.3    Muthiah, T.P.4
  • 30
    • 0030954878 scopus 로고    scopus 로고
    • Crystal structure and resonance Raman studies of protocatechuate 3,4-dioxygenase complexed with 3,4-dihydroxyphenylacetate
    • T.E. Elgren, A.M. Orville, K.A. Kelly, J.D. Lipscomb, D.H. Ohlendorf, and L. Que Jr. Crystal structure and resonance Raman studies of protocatechuate 3,4-dioxygenase complexed with 3,4-dihydroxyphenylacetate Biochemistry 36 1997 11504 11513
    • (1997) Biochemistry , vol.36 , pp. 11504-11513
    • Elgren, T.E.1    Orville, A.M.2    Kelly, K.A.3    Lipscomb, J.D.4    Ohlendorf, D.H.5    Que Jr., L.6
  • 31
    • 0034636805 scopus 로고    scopus 로고
    • Structure of Acinetobacter calcoaceticus protocatechuate 3,4-dioxygenase at 2.2 Å resolution: Implications for the mechanism of an intradiol dioxygenase
    • M.W. Vetting, D.A. D'Argenio, L.N. Ornston, and D.H. Ohlendorf Structure of Acinetobacter calcoaceticus protocatechuate 3,4-dioxygenase at 2.2 Å resolution: Implications for the mechanism of an intradiol dioxygenase Biochemistry 39 2000 7943 7955
    • (2000) Biochemistry , vol.39 , pp. 7943-7955
    • Vetting, M.W.1    D'Argenio, D.A.2    Ornston, L.N.3    Ohlendorf, D.H.4
  • 32
    • 0016806798 scopus 로고
    • Extradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, pyrocatechase, from a Pseudomonad
    • M. Fujiwara, L.A. Golovleva, Y. Saeki, M. Nozaki, and O. Hayaishi Extradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, pyrocatechase, from a Pseudomonad J. Biol. Chem. 250 1975 4848 4855
    • (1975) J. Biol. Chem. , vol.250 , pp. 4848-4855
    • Fujiwara, M.1    Golovleva, L.A.2    Saeki, Y.3    Nozaki, M.4    Hayaishi, O.5
  • 33
    • 0032190167 scopus 로고    scopus 로고
    • Quantitative structure/activity relationship for the rate of conversion of C4-substituted catechols by catechol-1,2-dioxygenase from Pseudomonas putida (arvilla) C1
    • L. Ridder, F. Briganti, M.G. Boersma, S. Boeren, E.H. Vis, A. Scozzafava, C. Veeger, and I.M. Rietjens Quantitative structure/activity relationship for the rate of conversion of C4-substituted catechols by catechol-1,2-dioxygenase from Pseudomonas putida (arvilla) C1 Eur. J. Biochem. 257 1998 92 100
    • (1998) Eur. J. Biochem. , vol.257 , pp. 92-100
    • Ridder, L.1    Briganti, F.2    Boersma, M.G.3    Boeren, S.4    Vis, E.H.5    Scozzafava, A.6    Veeger, C.7    Rietjens, I.M.8
  • 34
    • 0017814391 scopus 로고
    • Chemical structure and biodegradability of halogenated aromatic compounds. Substituent effects on 1,2-dioxygenation of catechol
    • E. Dorn, and H.J. Knackmuss Chemical structure and biodegradability of halogenated aromatic compounds. Substituent effects on 1,2-dioxygenation of catechol Biochem. J. 174 1978 85 94
    • (1978) Biochem. J. , vol.174 , pp. 85-94
    • Dorn, E.1    Knackmuss, H.J.2
  • 35
    • 0032718514 scopus 로고    scopus 로고
    • Substitution, insertion, deletion, suppression, and altered substrate specificity in functional protocatechuate 3,4-dioxygenases
    • D.A. D'Argenio, M.W. Vetting, D.H. Ohlendorf, and L.N. Ornston Substitution, insertion, deletion, suppression, and altered substrate specificity in functional protocatechuate 3,4-dioxygenases J. Bacteriol. 181 1999 6478 6487
    • (1999) J. Bacteriol. , vol.181 , pp. 6478-6487
    • D'Argenio, D.A.1    Vetting, M.W.2    Ohlendorf, D.H.3    Ornston, L.N.4
  • 36
    • 0015501407 scopus 로고
    • Protocatechuate 3,4-dioxygenase. III. An oxygenated form of enzyme as reaction intermediate
    • H. Fujisawa, K. Hiromi, M. Uyeda, S. Okuno, and M. Nozaki Protocatechuate 3,4-dioxygenase. III. An oxygenated form of enzyme as reaction intermediate J. Biol. Chem. 247 1972 4422 4428
    • (1972) J. Biol. Chem. , vol.247 , pp. 4422-4428
    • Fujisawa, H.1    Hiromi, K.2    Uyeda, M.3    Okuno, S.4    Nozaki, M.5
  • 37
    • 0032562027 scopus 로고    scopus 로고
    • 3+ ligand in protocatechuate 3,4-dioxygenase influences substrate binding and product release: Evidence for new reaction cycle intermediates
    • 3+ ligand in protocatechuate 3,4-dioxygenase influences substrate binding and product release: evidence for new reaction cycle intermediates Biochemistry 37 1998 2131 2144
    • (1998) Biochemistry , vol.37 , pp. 2131-2144
    • Frazee, R.W.1    Orville, A.M.2    Dolbeare, K.B.3    Yu, H.4    Ohlendorf, D.H.5    Lipscomb, J.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.