메뉴 건너뛰기




Volumn 286, Issue 1, 1999, Pages 135-149

Structure of catalase-A from Saccharomyces cerevisiae

Author keywords

Heme; Molecular channels; NADPH; Stability; X ray structure

Indexed keywords

CATALASE; HEME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0033548124     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2453     Document Type: Article
Times cited : (101)

References (57)
  • 1
    • 0025239770 scopus 로고
    • Inactivation of peroxidase by hydrogen peroxide and its protection by a reducing agent
    • Arnao M. B., Acosta M., del Rio J. A., García-Canovas F. Inactivation of peroxidase by hydrogen peroxide and its protection by a reducing agent. Biochim. Biophys. Acta. 1038:1990;85-89.
    • (1990) Biochim. Biophys. Acta , vol.1038 , pp. 85-89
    • Arnao, M.B.1    Acosta, M.2    Del Rio, J.A.3    García-Canovas, F.4
  • 2
    • 0027207715 scopus 로고
    • On the mechanism of peroxidase-catalyzed oxygen production
    • Barr D. P., Aust S. D. On the mechanism of peroxidase-catalyzed oxygen production. Arch. Biochem. Biophys. 303:1993;377-382.
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 377-382
    • Barr, D.P.1    Aust, S.D.2
  • 4
    • 0030807274 scopus 로고    scopus 로고
    • Unusual conformation of nicotinamide adenine dinucleotide (NAD) bound to diphteria toxin: A comparison with NAD bound to the oxidorreductases enzymes
    • Bell C. E., Yeates T. O., Eisenberg D. Unusual conformation of nicotinamide adenine dinucleotide (NAD) bound to diphteria toxin: a comparison with NAD bound to the oxidorreductases enzymes. Protein Sci. 6:1997;2084-2096.
    • (1997) Protein Sci. , vol.6 , pp. 2084-2096
    • Bell, C.E.1    Yeates, T.O.2    Eisenberg, D.3
  • 6
    • 0029089392 scopus 로고
    • Simulations of electron transfer in the NADPH-bound catalase from Proteus mirabilis PR
    • Bicout D. J., Field M. J., Gouet P., Jouve H. M. Simulations of electron transfer in the NADPH-bound catalase from Proteus mirabilis PR. Biochim. Biophys. Acta. 1252:1995;172-176.
    • (1995) Biochim. Biophys. Acta , vol.1252 , pp. 172-176
    • Bicout, D.J.1    Field, M.J.2    Gouet, P.3    Jouve, H.M.4
  • 7
    • 0025868939 scopus 로고
    • Vector-mediated overexpression of catalase A in the yeast Saccharomyces cerevisiae induces inclusion body formation
    • Binder M., Schanz M., Hartig A. Vector-mediated overexpression of catalase A in the yeast Saccharomyces cerevisiae induces inclusion body formation. Eur. J. Cell. Biol. 54:1991;305-312.
    • (1991) Eur. J. Cell. Biol. , vol.54 , pp. 305-312
    • Binder, M.1    Schanz, M.2    Hartig, A.3
  • 9
    • 0015442713 scopus 로고
    • Polarographic determination of diffusion coefficients of hydrogen peroxide and iron chelates and rate constants of hydroxyl radical reactions
    • Borggaard O. K. Polarographic determination of diffusion coefficients of hydrogen peroxide and iron chelates and rate constants of hydroxyl radical reactions. Acta Chem. Scand. 26:1972;3393-3394.
    • (1972) Acta Chem. Scand. , vol.26 , pp. 3393-3394
    • Borggaard, O.K.1
  • 11
    • 0030945035 scopus 로고    scopus 로고
    • Identification of a novel bond between a histine and the essential tyrosine in catalase HPII of Escherichia coli
    • Bravo J., Fita I., Ferrer J. C., Ens W., Hillar A., Switala J., Loewen P. C. Identification of a novel bond between a histine and the essential tyrosine in catalase HPII of Escherichia coli. Protein Sci. 6:1997a;1016-1023.
    • (1997) Protein Sci. , vol.6 , pp. 1016-1023
    • Bravo, J.1    Fita, I.2    Ferrer, J.C.3    Ens, W.4    Hillar, A.5    Switala, J.6    Loewen, P.C.7
  • 14
    • 0001423896 scopus 로고
    • Effect of pH upon the reaction kinetics of the enzyme-substrate compounds of catalase
    • Chance B. Effect of pH upon the reaction kinetics of the enzyme-substrate compounds of catalase. J. Biol. Chem. 194:1952;471-481.
    • (1952) J. Biol. Chem. , vol.194 , pp. 471-481
    • Chance, B.1
  • 15
    • 0001113307 scopus 로고
    • The enzyme-substrate compounds of bacterial catalase and peroxides
    • Chance B., Herbert D. The enzyme-substrate compounds of bacterial catalase and peroxides. Biochem. J. 46:1950;402-414.
    • (1950) Biochem. J. , vol.46 , pp. 402-414
    • Chance, B.1    Herbert, D.2
  • 16
    • 0024431464 scopus 로고
    • Proposed structure for the prosthetic group of catalase HPII from Escherichia coli
    • Chiu J. T., Loewen P. C., Switala J., Gennis R. B., Timkovich R. Proposed structure for the prosthetic group of catalase HPII from Escherichia coli. J. Am. Chem. Soc. 111:1989;7046-7050.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 7046-7050
    • Chiu, J.T.1    Loewen, P.C.2    Switala, J.3    Gennis, R.B.4    Timkovich, R.5
  • 17
    • 84933948864 scopus 로고
    • Nonchromosomal antibiotic resistance in bacteria: Genetic transformation of Escherichia coli by R -factor DNA
    • Cohen S. N., Chang A. C. J., Hsu I. Nonchromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R -factor DNA. Proc. Natl Acad. Sci. USA. 75:1972;1929-1933.
    • (1972) Proc. Natl Acad. Sci. USA , vol.75 , pp. 1929-1933
    • Cohen, S.N.1    Chang, A.C.J.2    Hsu, I.3
  • 22
    • 0022179287 scopus 로고
    • The active center of catalase
    • Fita I., Rossmann M. G. The active center of catalase. J. Mol. Biol. 185:1985;21-37.
    • (1985) J. Mol. Biol. , vol.185 , pp. 21-37
    • Fita, I.1    Rossmann, M.G.2
  • 24
    • 0030047892 scopus 로고    scopus 로고
    • Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissium
    • Fraaije M. W., Roubroeks H. P., Hagen W. R., Van Berkel W. J. H. Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissium. Eur. J. Biochem. 235:1996;192-198.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 192-198
    • Fraaije, M.W.1    Roubroeks, H.P.2    Hagen, W.R.3    Van Berkel, W.J.H.4
  • 25
    • 0029001848 scopus 로고
    • Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH
    • Gouet P., Jouve H. M., Dideberg O. Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH. J. Mol. Biol. 249:1995;933-954.
    • (1995) J. Mol. Biol. , vol.249 , pp. 933-954
    • Gouet, P.1    Jouve, H.M.2    Dideberg, O.3
  • 27
    • 0025972738 scopus 로고
    • DNA damage by oxygen-derived species
    • Halliwell B., Aruoma O. I. DNA damage by oxygen-derived species. FEBS Letters. 281:1991;9-19.
    • (1991) FEBS Letters , vol.281 , pp. 9-19
    • Halliwell, B.1    Aruoma, O.I.2
  • 28
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human deseases
    • Halliwell B., Gutteridge J. M. C. Role of free radicals and catalytic metal ions in human deseases. Methods Enzymol. 186:1990;1-90.
    • (1990) Methods Enzymol. , vol.186 , pp. 1-90
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 29
    • 0344437691 scopus 로고    scopus 로고
    • Function of NADPH in catalase A from Saccharomyces cerevisiae
    • Herzog C., Zamocky M., Nykyri L., Koller F. Function of NADPH in catalase A from Saccharomyces cerevisiae. Protein Sci. 6:1997;S106.
    • (1997) Protein Sci. , vol.6 , pp. 106
    • Herzog, C.1    Zamocky, M.2    Nykyri, L.3    Koller, F.4
  • 30
    • 0001823786 scopus 로고
    • Recombinat PCR
    • M. A. Innis, D. H. Gelfand, J. J. Sninsky, & T. J. White. San Diego: Academic Press
    • Higuchi R. Recombinat PCR. Innis M. A., Gelfand D. H., Sninsky J. J., White T. J. PCR protocols. 1990;177-183 Academic Press, San Diego.
    • (1990) PCR Protocols , pp. 177-183
    • Higuchi, R.1
  • 31
    • 0026470233 scopus 로고
    • A mechanism for NADPH inhibition of catalase compound II formation
    • Hillar A., Nicholls P. A mechanism for NADPH inhibition of catalase compound II formation. FEBS Letters. 314:1992;179-182.
    • (1992) FEBS Letters , vol.314 , pp. 179-182
    • Hillar, A.1    Nicholls, P.2
  • 32
    • 0030835382 scopus 로고    scopus 로고
    • EPR investigation of compound I in Proteus mirabilis and bovine liver catalase: Formation of porphyrin and tyrosil radical intermediates
    • Ivancich A., Jouve H. M., Sartor B., Gaillard J. EPR investigation of compound I in Proteus mirabilis and bovine liver catalase: formation of porphyrin and tyrosil radical intermediates. Biochemistry. 36:1997;9356-9364.
    • (1997) Biochemistry , vol.36 , pp. 9356-9364
    • Ivancich, A.1    Jouve, H.M.2    Sartor, B.3    Gaillard, J.4
  • 33
    • 0029844594 scopus 로고    scopus 로고
    • Importance of catalase in the adaptative response to hydrogen peroxide: Analysis of acatalasaemic Saccharomyces cerevisiae
    • Izawa S., Inoue Y., Kimura A. Importance of catalase in the adaptative response to hydrogen peroxide: analysis of acatalasaemic Saccharomyces cerevisiae. Biochem. J. 320:1996;61-67.
    • (1996) Biochem. J. , vol.320 , pp. 61-67
    • Izawa, S.1    Inoue, Y.2    Kimura, A.3
  • 34
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T. A., Zon J. Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystalog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystalog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zon, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 35
    • 0027299188 scopus 로고
    • The stucture of human carbonic anhydrase II in complex with bromide and azide
    • Jönsson B. M., Häkansson K., Liljas A. The stucture of human carbonic anhydrase II in complex with bromide and azide. FEBS Letters. 322:1993;186-190.
    • (1993) FEBS Letters , vol.322 , pp. 186-190
    • Jönsson, B.M.1    Häkansson, K.2    Liljas, A.3
  • 38
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecules structures
    • Kleywegt G. J., Jones T. A. Detection, delineation, measurement and display of cavities in macromolecules structures. Acta Crystallog. sect. D. 50:1994;178-185.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 39
    • 0030854046 scopus 로고    scopus 로고
    • Phylogenetic relationships among prokaryotic and eukaryotic catalases
    • Klotz M. G., Klassen G. R., Loewen P. C. Phylogenetic relationships among prokaryotic and eukaryotic catalases. Mol. Biol. Evol. 14:1997;951-958.
    • (1997) Mol. Biol. Evol. , vol.14 , pp. 951-958
    • Klotz, M.G.1    Klassen, G.R.2    Loewen, P.C.3
  • 40
    • 0028082682 scopus 로고
    • Characterization of hydrogen peroxide and superoxide degrading pathways of Aspergillus niger catalase: A steady-state analysis
    • Lardinois O. M., Rouxhet P. G. Characterization of hydrogen peroxide and superoxide degrading pathways of Aspergillus niger catalase: a steady-state analysis. Free Radic. Res. 20:1994;29-50.
    • (1994) Free Radic. Res. , vol.20 , pp. 29-50
    • Lardinois, O.M.1    Rouxhet, P.G.2
  • 41
    • 0030090778 scopus 로고    scopus 로고
    • The kinetic and catalytic properties of Penicillium vitale catalase
    • Latyshko N. V., Gudkova L. K. The kinetic and catalytic properties of Penicillium vitale catalase. Ukr. Biochim. Zh. 68:1996;69-73.
    • (1996) Ukr. Biochim. Zh. , vol.68 , pp. 69-73
    • Latyshko, N.V.1    Gudkova, L.K.2
  • 42
    • 0027499128 scopus 로고
    • Increased serum catalase activity in rats subjected to thermal skin injury
    • Leff J. A. Increased serum catalase activity in rats subjected to thermal skin injury. Inflammation. 17:1993;199-204.
    • (1993) Inflammation , vol.17 , pp. 199-204
    • Leff, J.A.1
  • 47
    • 0001408791 scopus 로고
    • Catalases
    • P. D. Boyer. New York: Academic Press
    • Nicholls P., Schonbaum G. R. Catalases. Boyer P. D. The Enzymes. 1963;147-225 Academic Press, New York.
    • (1963) The Enzymes , pp. 147-225
    • Nicholls, P.1    Schonbaum, G.R.2
  • 48
    • 0031172190 scopus 로고    scopus 로고
    • Activity, peroxide compound formation, and heme d synthesis in Escherichia coli HPII catalase
    • Obinger C., Maj M., Nicholls P., Loewen P. C. Activity, peroxide compound formation, and heme d synthesis in Escherichia coli HPII catalase. Arch. Biochem. Biophys. 342:1997;58-67.
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 58-67
    • Obinger, C.1    Maj, M.2    Nicholls, P.3    Loewen, P.C.4
  • 49
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 50
    • 0000454621 scopus 로고    scopus 로고
    • Cell biology of yeast fungal catalases
    • J. G. Scandalious. Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Ruis H., Koller F. Cell biology of yeast fungal catalases. Scandalious J. G. Oxidative Stress and the Molecular Biology of Antioxidant Defenses. 1997;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1997) Oxidative Stress and the Molecular Biology of Antioxidant Defenses
    • Ruis, H.1    Koller, F.2
  • 51
    • 77956932249 scopus 로고
    • Catalase
    • P. D. Boyer. New York: Academic Press
    • Schonbaum G. R., Chance B. Catalase. Boyer P. D. The Enzymes. 1976;363-408 Academic Press, New York.
    • (1976) The Enzymes , pp. 363-408
    • Schonbaum, G.R.1    Chance, B.2
  • 52
    • 0015686845 scopus 로고
    • Novel catalitic proteins of bakers' yeast. I. An atypical catalase
    • Seah T. C. M., Bhatti A. R., Kaplan J. G. Novel catalitic proteins of bakers' yeast. I. An atypical catalase. Can. J. Biochem. 51:1973;1551-1555.
    • (1973) Can. J. Biochem. , vol.51 , pp. 1551-1555
    • Seah, T.C.M.1    Bhatti, A.R.2    Kaplan, J.G.3
  • 54
    • 0031879055 scopus 로고    scopus 로고
    • Truncation and heme pocket mutations reduce production of functional catalase HPII in Eschericchia coli
    • Sevinc M. S., Switala J., Bravo J., Fita I., Loewen P. C. Truncation and heme pocket mutations reduce production of functional catalase HPII in Eschericchia coli. Protein Eng. 11:1998;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
  • 56
    • 0028095182 scopus 로고
    • Buried waters and internal cavities in monomeric proteins
    • Williams M. A., Goodfellow J. M., Thornton J. M. Buried waters and internal cavities in monomeric proteins. Protein Sci. 3:1994;1224-1235.
    • (1994) Protein Sci. , vol.3 , pp. 1224-1235
    • Williams, M.A.1    Goodfellow, J.M.2    Thornton, J.M.3
  • 57
    • 0029020576 scopus 로고
    • Site-directed mutagenesis of the lower parts of the major substrate channel of yeast catalase A leads to highly increased peroxidatic activity
    • Zamocky M., Herzog C., Nykyri L. M., Koller F. Site-directed mutagenesis of the lower parts of the major substrate channel of yeast catalase A leads to highly increased peroxidatic activity. FEBS Letters. 367:1995;241-245.
    • (1995) FEBS Letters , vol.367 , pp. 241-245
    • Zamocky, M.1    Herzog, C.2    Nykyri, L.M.3    Koller, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.