메뉴 건너뛰기




Volumn 20, Issue 2, 2005, Pages 131-135

Catalase: A repertoire of unusual features

Author keywords

Aquaporins; Catalases; Channels

Indexed keywords

ANTIOXIDANT; AQUAPORIN; CARRIER PROTEIN; CATALASE; GLYCEROL; HEME; MEMBRANE PROTEIN; PORIN; WATER;

EID: 24044470984     PISSN: 09701915     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02867412     Document Type: Review
Times cited : (27)

References (35)
  • 1
    • 0032924755 scopus 로고    scopus 로고
    • Resistance to nitric oxide-mediated apoptosis in HL-60 variant cells is associated with increased activities of Cu.Zn-superoxide dismutase and catalase
    • Yabuki, M., Kariya, S., Ishisaka, R., Yasuda, T., Yoshioka, T., Norton, A.A. and Utsumi, K. (1999) Resistance to nitric oxide-mediated apoptosis in HL-60 variant cells is associated with increased activities of Cu.Zn-superoxide dismutase and catalase. Free Radic. Biol. Med. 26 (3-4), 325-332.
    • (1999) Free Radic. Biol. Med. , vol.26 , Issue.3-4 , pp. 325-332
    • Yabuki, M.1    Kariya, S.2    Ishisaka, R.3    Yasuda, T.4    Yoshioka, T.5    Norton, A.A.6    Utsumi, K.7
  • 2
    • 0023235226 scopus 로고
    • Reduced oxygen species, mutation, induction and cancer initiation
    • Vuillaume, M. (1987) Reduced oxygen species, mutation, induction and cancer initiation. Mutat. Res. 186, 43-72.
    • (1987) Mutat. Res. , vol.186 , pp. 43-72
    • Vuillaume, M.1
  • 3
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell, B. and Gutteridge, J.M. (1984) Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J. 219 (1), 1-14.
    • (1984) Biochem J. , vol.219 , Issue.1 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.2
  • 4
    • 0029832625 scopus 로고    scopus 로고
    • Identification of a novel growth-promoting factor with a wide target cell spectrum from various tumor cells as catalase
    • Miyamoto, T, Hayashi, M., Takeuchi, A., Okamoto, T., Kawashima, S., Takii, T., Hayashi, H. and Onozaki, K. (1996) Identification of a novel growth-promoting factor with a wide target cell spectrum from various tumor cells as catalase. J. Biochem. (Tokyo), 120, 725-730.
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 725-730
    • Miyamoto, T.1    Hayashi, M.2    Takeuchi, A.3    Okamoto, T.4    Kawashima, S.5    Takii, T.6    Hayashi, H.7    Onozaki, K.8
  • 5
    • 0024595407 scopus 로고
    • Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes
    • Gaetani, G.F., Galiano, S., Canepa, L., Ferraris, A.M. and Kirkman, H.N. (1989) Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes. Blood 73 (1), 334-339.
    • (1989) Blood , vol.73 , Issue.1 , pp. 334-339
    • Gaetani, G.F.1    Galiano, S.2    Canepa, L.3    Ferraris, A.M.4    Kirkman, H.N.5
  • 10
    • 0027439322 scopus 로고
    • Catalase HPII of Escherichia coli catalyzes the conversion of protoheme to cis-heme d
    • Loewen, P.C., Switala, J., von Ossowski, I., Hillar, A., Christie, A., Tattrie, B., et al. (1993) Catalase HPII of Escherichia coli catalyzes the conversion of protoheme to cis-heme d. Biochemistry 32, 10159-10164.
    • (1993) Biochemistry , vol.32 , pp. 10159-10164
    • Loewen, P.C.1    Switala, J.2    Von Ossowski, I.3    Hillar, A.4    Christie, A.5    Tattrie, B.6
  • 11
    • 0031879055 scopus 로고    scopus 로고
    • Truncation and heme pocket mutations reduce production of functional catalase HPII in Escherichia coli
    • Sevinc, M.S., Switala, J., Bravo, J., Fita, I. and Loewen, P. C. (1998) Truncation and heme pocket mutations reduce production of functional catalase HPII in Escherichia coli. Protein Eng. 11, 549-555.
    • (1998) Protein Eng. , vol.11 , pp. 549-555
    • Sevinc, M.S.1    Switala, J.2    Bravo, J.3    Fita, I.4    Loewen, P.C.5
  • 12
    • 0031569328 scopus 로고    scopus 로고
    • Proline-dependent oligomerization with arm exchange
    • Bergdoll, M., Remy, M.H., Cagnon, C., Masson, J.M. and Dumas P. (1997) Proline-dependent oligomerization with arm exchange. Structure 5 (3), 391-401.
    • (1997) Structure , vol.5 , Issue.3 , pp. 391-401
    • Bergdoll, M.1    Remy, M.H.2    Cagnon, C.3    Masson, J.M.4    Dumas, P.5
  • 13
    • 0038236523 scopus 로고    scopus 로고
    • Structure-function study of the amino-terminal stretch of the catalase subunit molecule in oligomerization, heme binding, and activity expression
    • Ueda, M., Kinoshita, H., Maeda, S.I., Zou, W. and Tanaka, A. (2003) Structure-function study of the amino-terminal stretch of the catalase subunit molecule in oligomerization, heme binding, and activity expression. Appl. Microbiol. Biotechnol. 61 (5-6), 488-494.
    • (2003) Appl. Microbiol. Biotechnol. , vol.61 , Issue.5-6 , pp. 488-494
    • Ueda, M.1    Kinoshita, H.2    Maeda, S.I.3    Zou, W.4    Tanaka, A.5
  • 14
    • 0037297450 scopus 로고    scopus 로고
    • High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron
    • Andreoletti, P., Sainz, G., Jaquinod, M., Gagnon, J. and Jouve H.M. (2003) High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron. Proteins. 50, 261-271.
    • (2003) Proteins. , vol.50 , pp. 261-271
    • Andreoletti, P.1    Sainz, G.2    Jaquinod, M.3    Gagnon, J.4    Jouve, H.M.5
  • 15
    • 0037614920 scopus 로고    scopus 로고
    • Hydroperoxidase Il of Escherichia coli exhibits enhanced resistance to proteolytic cleavage compared to other catalases
    • Chelikani, P., Donald, L. J., Duckworth, H. W. and Loewen P.C. (2003) Hydroperoxidase Il of Escherichia coli Exhibits Enhanced Resistance to Proteolytic Cleavage Compared to Other Catalases. Biochemistry. 42, 5729-5735.
    • (2003) Biochemistry , vol.42 , pp. 5729-5735
    • Chelikani, P.1    Donald, L.J.2    Duckworth, H.W.3    Loewen, P.C.4
  • 17
    • 0033616493 scopus 로고    scopus 로고
    • Catalase HPII from Escherichia coli exhibits enhanced resistance to denaturation
    • Switala, J., O'Neil, J. O. and Loewen, P. C. (1999) Catalase HPII from Escherichia coli exhibits enhanced resistance to denaturation. Biochemistry 38, 3895-3901.
    • (1999) Biochemistry , vol.38 , pp. 3895-3901
    • Switala, J.1    O'Neil, J.O.2    Loewen, P.C.3
  • 20
    • 0029001848 scopus 로고
    • Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH
    • Gouet, P., Jouve, H. M. and Dideberg O. (1995) Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH. J. Mol. Biol. 249, 933-954.
    • (1995) J. Mol. Biol. , vol.249 , pp. 933-954
    • Gouet, P.1    Jouve, H.M.2    Dideberg, O.3
  • 22
    • 0034635333 scopus 로고    scopus 로고
    • Active and inhibited human catalase sturctures: Ligand and NADPH binding and catalytic mechanism
    • Putnam, C.D., Arvai, A.S., Bourne, Y. and Tainer, J.A. (1999) Active and inhibited human catalase sturctures: ligand and NADPH binding and catalytic mechanism. J. Mol. Biol. 296, 295-309.
    • (1999) J. Mol. Biol. , vol.296 , pp. 295-309
    • Putnam, C.D.1    Arvai, A.S.2    Bourne, Y.3    Tainer, J.A.4
  • 28
    • 85039372606 scopus 로고    scopus 로고
    • nobelprize.org/chemistry/laureates/2003
    • Noble Lectures 2003 (nobelprize.org/chemistry/ laureates/2003/).
    • (2003) Noble Lectures
  • 29
    • 0034919604 scopus 로고    scopus 로고
    • Channeling of substrates and intermediates in enzyme-catalyzed reactions
    • Huang, X., Holden, H.M. and Raushel, F.M. (2001) Channeling of substrates and intermediates in enzyme-catalyzed reactions. Annu. Rev. Biochem. 70, 149-180.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 149-180
    • Huang, X.1    Holden, H.M.2    Raushel, F.M.3
  • 31
    • 0043234246 scopus 로고    scopus 로고
    • An electrical potential in the access channel of catalases enhances catalysis
    • Chelikani, P., Carpena, X., Fita, I. and Loewen, P.C. (2003) An electrical potential in the access channel of catalases enhances catalysis. J. Biol. Chem. 278 (33), 31290-31296.
    • (2003) J. Biol. Chem. , vol.278 , Issue.33 , pp. 31290-31296
    • Chelikani, P.1    Carpena, X.2    Fita, I.3    Loewen, P.C.4
  • 33
    • 0035802360 scopus 로고    scopus 로고
    • Theoretical study of the mechanisms of substrate recognition by catalase
    • Kalko, S.G., Gelpi, J.L., Fita, I. and Orozco, M. (2001) Theoretical study of the mechanisms of substrate recognition by catalase. J. Amer. Chem. Soc. 123, 9665-9672.
    • (2001) J. Amer. Chem. Soc. , vol.123 , pp. 9665-9672
    • Kalko, S.G.1    Gelpi, J.L.2    Fita, I.3    Orozco, M.4
  • 34
    • 0034813458 scopus 로고    scopus 로고
    • Ligand diffusion in the catalase from Proteus mirabilis: A molecular dynamics study
    • Amara, P., Andreoletti, P., Jouve, H. M. and Field, M. J. (2001) Ligand diffusion in the catalase from Proteus mirabilis: A molecular dynamics study. Protein Sci. 10, 1927-1935.
    • (2001) Protein Sci. , vol.10 , pp. 1927-1935
    • Amara, P.1    Andreoletti, P.2    Jouve, H.M.3    Field, M.J.4
  • 35
    • 79251629140 scopus 로고
    • The influence of chymotrypsin and pepsin on beef liver catalase and horse radish peroxidase
    • Radhakrishnan, T. M., Raghupathy, E. and Sarma P.S. (1963) The influence of chymotrypsin and pepsin on beef liver catalase and horse radish peroxidase. Ind. J. Chem. 1, 40-43.
    • (1963) Ind. J. Chem. , vol.1 , pp. 40-43
    • Radhakrishnan, T.M.1    Raghupathy, E.2    Sarma, P.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.