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Volumn 122, Issue 1, 1997, Pages 201-204

Crystallization and preliminary X-ray diffraction studies of expressed Pseudomonas putida catechol 2,3-dioxygenase

Author keywords

Catechol 2,3 dioxygenase; Crystallization; Metapyrocatechase; Non heme iron dioxygenase; X ray crystallography

Indexed keywords

ALCOHOL; BACTERIAL ENZYME; CATECHOL; CATECHOL 1,2 DIOXYGENASE; CITRATE SODIUM; FERROUS ION; OXYGENASE;

EID: 0030795859     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021729     Document Type: Article
Times cited : (8)

References (18)
  • 1
    • 78651128288 scopus 로고
    • Metapyrocatechase: A new catechol-cleaving enzyme
    • Kojima, Y., Itada, N., and Hayaishi, O. (1961) Metapyrocatechase: a new catechol-cleaving enzyme. J. Biol. Chem. 236, 2223-2228
    • (1961) J. Biol. Chem. , vol.236 , pp. 2223-2228
    • Kojima, Y.1    Itada, N.2    Hayaishi, O.3
  • 2
    • 0021099237 scopus 로고
    • Purification, subunit structure, and partial amino acid sequence of metapyrocatechase
    • Nakai, C., Hori, K., Kagamiyama, H., Nakazawa, T., and Nozaki, M. (1983) Purification, subunit structure, and partial amino acid sequence of metapyrocatechase. J. Biol. Chem. 258, 2916-2922
    • (1983) J. Biol. Chem. , vol.258 , pp. 2916-2922
    • Nakai, C.1    Hori, K.2    Kagamiyama, H.3    Nakazawa, T.4    Nozaki, M.5
  • 3
    • 0020560883 scopus 로고
    • Complete nucleotide sequence of the metapyrocatechase gene on the TOL plasmid of Pseudomonas putida mt-2
    • Nakai, C., Kagamiyama, H., Nozaki, M., Nakazawa, T., Inouye, S., Ebina, Y., and Nakazawa, A. (1983) Complete nucleotide sequence of the metapyrocatechase gene on the TOL plasmid of Pseudomonas putida mt-2. J. Biol. Chem. 258, 2923-2928
    • (1983) J. Biol. Chem. , vol.258 , pp. 2923-2928
    • Nakai, C.1    Kagamiyama, H.2    Nozaki, M.3    Nakazawa, T.4    Inouye, S.5    Ebina, Y.6    Nakazawa, A.7
  • 4
    • 78651128985 scopus 로고
    • Metapyrocatechase. I. Purification, crystallization and some properties
    • Nozaki, M., Kagamiyama, H., and Hayaishi, O. (1963) Metapyrocatechase. I. Purification, crystallization and some properties. Biochem. Z. 338, 582-590
    • (1963) Biochem. Z. , vol.338 , pp. 582-590
    • Nozaki, M.1    Kagamiyama, H.2    Hayaishi, O.3
  • 5
    • 0014429573 scopus 로고
    • Metapyrocatechase. II. The role of iron and sulfhydryl groups
    • Nozaki, M., Ono, K., Nakagawa, T., Kotani, S., and Hayaishi, O. (1968) Metapyrocatechase. II. The role of iron and sulfhydryl groups. J. Biol. Chem. 243, 2682-2690
    • (1968) J. Biol. Chem. , vol.243 , pp. 2682-2690
    • Nozaki, M.1    Ono, K.2    Nakagawa, T.3    Kotani, S.4    Hayaishi, O.5
  • 6
    • 0028988356 scopus 로고
    • Overexpression of Pseudomonas putida catechol 2,3-dioxygenase with high specific activity by genetically engineered Escherichia coli
    • Kobayashi, T., Ishida, T., Horiike, K., Takahara, Y., Numao, N., Nakazawa, A., Nakazawa, T., and Nozaki, M. (1995) Overexpression of Pseudomonas putida catechol 2,3-dioxygenase with high specific activity by genetically engineered Escherichia coli. J. Biochem. 117, 614-622
    • (1995) J. Biochem. , vol.117 , pp. 614-622
    • Kobayashi, T.1    Ishida, T.2    Horiike, K.3    Takahara, Y.4    Numao, N.5    Nakazawa, A.6    Nakazawa, T.7    Nozaki, M.8
  • 7
    • 0024296029 scopus 로고
    • Structure and assembly of protocatechuate 3,4-dioxygenase
    • Ohlendorf, D.H., Lipscomb, J.D., and Weber, P.C. (1988) Structure and assembly of protocatechuate 3,4-dioxygenase. Nature 336, 403-405
    • (1988) Nature , vol.336 , pp. 403-405
    • Ohlendorf, D.H.1    Lipscomb, J.D.2    Weber, P.C.3
  • 8
    • 0028067892 scopus 로고
    • Structure of protocatechuase 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 A resolution
    • Ohlendorf, D.H., Orville, A.M., and Lipscomb, J.D. (1994) Structure of protocatechuase 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 A resolution. J. Mol. Biol. 244, 586-608
    • (1994) J. Mol. Biol. , vol.244 , pp. 586-608
    • Ohlendorf, D.H.1    Orville, A.M.2    Lipscomb, J.D.3
  • 9
    • 0027246677 scopus 로고
    • The three-dimensional structure of an arachidonic acid 15-lipoxygenase
    • Boyington, J.C., Gaffney, B.J., and Amzel, L.M. (1993) The three-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
  • 10
    • 0002955249 scopus 로고
    • Three-dimensional structure of 2,3-dihydroxybiphenyl dioxygenase (BphC enzyme) from Pseudomonas sp. strain KKS102 having polychlorinated biphenyl degrading activity
    • Sugiyama, K., Senda, T., Narita, H., Yamamoto, T., Kimbara, K., Fukuda, M., Yano, K., and Mitsui, Y. (1995) Three-dimensional structure of 2,3-dihydroxybiphenyl dioxygenase (BphC enzyme) from Pseudomonas sp. strain KKS102 having polychlorinated biphenyl degrading activity. Proc. Jpn. Acad. 71B, 32-35
    • (1995) Proc. Jpn. Acad. , vol.71 B , pp. 32-35
    • Sugiyama, K.1    Senda, T.2    Narita, H.3    Yamamoto, T.4    Kimbara, K.5    Fukuda, M.6    Yano, K.7    Mitsui, Y.8
  • 11
    • 0030008087 scopus 로고    scopus 로고
    • Three-dimensional structure of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102
    • Senda, T., Sugiyama, K., Narita, H., Yamamoto, T., Kimbara, K., Fukuda, M., Sato, M., Yano, K., and Mitsui, Y. (1996) Three-dimensional structure of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102. J. Mol. Biol. 255, 735-752
    • (1996) J. Mol. Biol. , vol.255 , pp. 735-752
    • Senda, T.1    Sugiyama, K.2    Narita, H.3    Yamamoto, T.4    Kimbara, K.5    Fukuda, M.6    Sato, M.7    Yano, K.8    Mitsui, Y.9
  • 12
    • 0028862027 scopus 로고
    • Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad
    • Han, S., Eltis, L.D., Timmis, K.N., Muchmore, S.W., and Bolin, J.T. (1995) Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science 270, 976-980
    • (1995) Science , vol.270 , pp. 976-980
    • Han, S.1    Eltis, L.D.2    Timmis, K.N.3    Muchmore, S.W.4    Bolin, J.T.5
  • 14
    • 0000293676 scopus 로고
    • X-ray diffraction data collection system for modern protein crystallography with Weissenberg camera and an imaging plate using synchrotron radiation
    • Sakabe, N. (1991) X-ray diffraction data collection system for modern protein crystallography with Weissenberg camera and an imaging plate using synchrotron radiation. Nucl. Instrum. Methods A303, 448-463
    • (1991) Nucl. Instrum. Methods , vol.A303 , pp. 448-463
    • Sakabe, N.1
  • 15
  • 16
    • 0002193613 scopus 로고
    • The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallography
    • Higashi, T. (1989) The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallography. J. Appl. Crystallogr. 22, 9-18
    • (1989) J. Appl. Crystallogr. , vol.22 , pp. 9-18
    • Higashi, T.1
  • 18
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. (1968) Solvent content of protein crystals. J. Mol. Biol. 33, 494-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 494-497
    • Matthews, B.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.