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Volumn 248, Issue 3, 1997, Pages 889-896

Purification and characterization of an alcohol: N,N-dimethyl-4-nitrosoaniline oxidoreductase from the methanogen Methanosarcina barkeri DSM 804 strain Fusaro

Author keywords

Alcohol dehydrogenase; Aldehyde dismutation; Methanosarcina barkeri; N,N dimethyl 4 nitrosoaniline; Nicotinoprotein

Indexed keywords

ALCOHOL DEHYDROGENASE; OXIDOREDUCTASE;

EID: 0030794766     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00889.x     Document Type: Article
Times cited : (12)

References (33)
  • 1
    • 0028603326 scopus 로고
    • Metabolism of methanogens
    • Blaut, M. (1994) Metabolism of methanogens, Antonie van Leeuwenhoek 66, 187-208.
    • (1994) Antonie van Leeuwenhoek , vol.66 , pp. 187-208
    • Blaut, M.1
  • 2
    • 0029967858 scopus 로고    scopus 로고
    • Pathways of energy conservation in methanogenic archaea
    • Deppenmeier, U., Müller, V. & Gottschalk, G. (1996) Pathways of energy conservation in methanogenic archaea, Arch. Microbiol. 165, 149-163.
    • (1996) Arch. Microbiol. , vol.165 , pp. 149-163
    • Deppenmeier, U.1    Müller, V.2    Gottschalk, G.3
  • 4
    • 0029744528 scopus 로고    scopus 로고
    • Methylcobamide:coenzyme M methyltransferase isoenzymes from Methanosarcina barkeri
    • LeClerc, G. M. & Grahame, D. A. (1996) Methylcobamide:coenzyme M methyltransferase isoenzymes from Methanosarcina barkeri, J. Biol. Chem. 271, 18725-18731.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18725-18731
    • LeClerc, G.M.1    Grahame, D.A.2
  • 5
    • 0029947391 scopus 로고    scopus 로고
    • Primary structure and properties of the formyltransferase from the mesophilic Methanosarcina barkeri: Comparison with the enzymes from thermophilic and hyperthermophilic methanogens
    • Kunow, J., Shima, S., Vorholt, J. A. & Thauer, R. K. (1996) Primary structure and properties of the formyltransferase from the mesophilic Methanosarcina barkeri: Comparison with the enzymes from thermophilic and hyperthermophilic methanogens, Arch. Microbiol. 165, 97-105.
    • (1996) Arch. Microbiol. , vol.165 , pp. 97-105
    • Kunow, J.1    Shima, S.2    Vorholt, J.A.3    Thauer, R.K.4
  • 6
    • 0029985246 scopus 로고    scopus 로고
    • Catalytic properties, molecular composition and sequence alignments of pyruvate: Ferredoxin oxidoreductase from the methanogenic archaeon Methanosarcina barkeri (strain Fusaro)
    • Bock, A. K., Kunow, J., Glasemacher, J. & Schönheit, P. (1996) Catalytic properties, molecular composition and sequence alignments of pyruvate: ferredoxin oxidoreductase from the methanogenic archaeon Methanosarcina barkeri (strain Fusaro), Eur. J. Biochem. 237, 35-44.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 35-44
    • Bock, A.K.1    Kunow, J.2    Glasemacher, J.3    Schönheit, P.4
  • 7
    • 0028911711 scopus 로고
    • Purification and characterization of 5-aminolevulinic acid dehydratase from Methanosarcina barkeri
    • Bhosale, S., Kshirsagar, D., Pawar, P., Yeole, T. & Ranade, D. (1995) Purification and characterization of 5-aminolevulinic acid dehydratase from Methanosarcina barkeri, FEMS Microbiol. Lett. 127, 151-155.
    • (1995) FEMS Microbiol. Lett. , vol.127 , pp. 151-155
    • Bhosale, S.1    Kshirsagar, D.2    Pawar, P.3    Yeole, T.4    Ranade, D.5
  • 8
    • 0011351733 scopus 로고
    • Oxidation of ethanol by methanogenic bacteria
    • Frimmer, U. & Widdel, F. (1989) Oxidation of ethanol by methanogenic bacteria, Arch. Microbiol. 152, 479-483.
    • (1989) Arch. Microbiol. , vol.152 , pp. 479-483
    • Frimmer, U.1    Widdel, F.2
  • 9
    • 0025923076 scopus 로고
    • +-dependent alcohol dehydrogenases of Methanogenium liminatans and Methanobacterium palustre, specific for secondary alcohols
    • +-dependent alcohol dehydrogenases of Methanogenium liminatans and Methanobacterium palustre, specific for secondary alcohols, Eur. J. Biochem. 200, 43-51.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 43-51
    • Bleicher, K.1    Winter, J.2
  • 10
    • 0001004327 scopus 로고
    • 120-specific enzyme from Methanogenium thermophilum strain TCI
    • 120-specific enzyme from Methanogenium thermophilum strain TCI, Arch. Microbiol. 152, 322-328.
    • (1989) Arch. Microbiol. , vol.152 , pp. 322-328
    • Widdel, F.1    Wolfe, R.S.2
  • 11
    • 0002315412 scopus 로고
    • Classification of secondary alcohol-utilizing methanogens including a new thermophilic isolate
    • Widdel, F., Rouvière, P. E. & Wolfe, R. S. (1988) Classification of secondary alcohol-utilizing methanogens including a new thermophilic isolate, Arch. Microbiol. 150, 477-481.
    • (1988) Arch. Microbiol. , vol.150 , pp. 477-481
    • Widdel, F.1    Rouvière, P.E.2    Wolfe, R.S.3
  • 12
    • 0028997349 scopus 로고
    • Characterization of the Rhodococcus sp. NI86/21 gene encoding alcohol:N,N′-dimethyl-4-nitrosoaniline oxidoreductase inducible by atrazine and thiocarbamate herbicides
    • Nagy, I., Verheijen, S., De Schrijver, A., Van Damme, J., Proost, P., Schoofs, G., Vanderleyden, J. & De Mot, R. (1995) Characterization of the Rhodococcus sp. NI86/21 gene encoding alcohol:N,N′-dimethyl-4-nitrosoaniline oxidoreductase inducible by atrazine and thiocarbamate herbicides, Arch. Microbiol. 163, 439-446.
    • (1995) Arch. Microbiol. , vol.163 , pp. 439-446
    • Nagy, I.1    Verheijen, S.2    De Schrijver, A.3    Van Damme, J.4    Proost, P.5    Schoofs, G.6    Vanderleyden, J.7    De Mot, R.8
  • 13
    • 0022483312 scopus 로고
    • Formaldehyde dismutase, a novel NAD-binding oxidoreductase from Pseudomonas putida F61
    • Kato, N., Yamagami, T., Shimao, M. & Sakazawa, C. (1986) Formaldehyde dismutase, a novel NAD-binding oxidoreductase from Pseudomonas putida F61, Eur. J. Biochem. 156, 59-64.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 59-64
    • Kato, N.1    Yamagami, T.2    Shimao, M.3    Sakazawa, C.4
  • 14
    • 0027414466 scopus 로고
    • Nicotinoprotein NAD(P)-containing| alcohol/aldehyde oxidoreductases. Purification and characterization of a novel type from Amycolatopsis methanolica
    • Van Ophem, P. W., van Beeumen, J. & Duine, J. A. (1993) Nicotinoprotein NAD(P)-containing| alcohol/aldehyde oxidoreductases. Purification and characterization of a novel type from Amycolatopsis methanolica, Eur. J. Biochem. 212, 819-826.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 819-826
    • Van Ophem, P.W.1    Van Beeumen, J.2    Duine, J.A.3
  • 16
    • 0027405767 scopus 로고
    • Election microscopic analysis and structural characterization of novel NADP(H)-containing methanol: N,N′-dimethyl-4-nitrosoaniline oxidoreductases from the gram-positive methylotrophic bacteria Amycolatopsis methanolica and Mycobacterium gastri MB19
    • Bystrykh, L. V., Vonck, J., van Bruggen, E. F. J., van Beeumen, J., Samyn, B., Govorukhina, N. I., Arfman, N., Duine, J. A. & Dijkhuizen, L. (1993) Election microscopic analysis and structural characterization of novel NADP(H)-containing methanol: N,N′-dimethyl-4-nitrosoaniline oxidoreductases from the gram-positive methylotrophic bacteria Amycolatopsis methanolica and Mycobacterium gastri MB19, J. Bacteriol. 175, 1814-1822.
    • (1993) J. Bacteriol. , vol.175 , pp. 1814-1822
    • Bystrykh, L.V.1    Vonck, J.2    Van Bruggen, E.F.J.3    Van Beeumen, J.4    Samyn, B.5    Govorukhina, N.I.6    Arfman, N.7    Duine, J.A.8    Dijkhuizen, L.9
  • 17
    • 10644224511 scopus 로고
    • Formation of methane by bacterial extracts
    • Wolin, E. A., Wolin, M. J. & Wolfe, R. S. (1963) Formation of methane by bacterial extracts, J. Biol. Chem. 238, 2882-2886.
    • (1963) J. Biol. Chem. , vol.238 , pp. 2882-2886
    • Wolin, E.A.1    Wolin, M.J.2    Wolfe, R.S.3
  • 18
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall, A. G., Bardawill, C. J. & David, M. M. (1949) Determination of serum proteins by means of the biuret reaction, J. Biol. Chem. 177, 751-766.
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantification of microgram quantities of protein using the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for quantification of microgram quantities of protein using the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0029205727 scopus 로고
    • Genomic nucleotide sequence of an Arabidopsis thaliana gene encoding a cinnamyl alcohol dehydrogenase
    • Baucher, M., van Doorsselaere, J., Gielen, J., van Montagu, M., Inze, D. & Boerjan, W. (1995) Genomic nucleotide sequence of an Arabidopsis thaliana gene encoding a cinnamyl alcohol dehydrogenase, Plant Physiol. 107, 285-286.
    • (1995) Plant Physiol. , vol.107 , pp. 285-286
    • Baucher, M.1    Van Doorsselaere, J.2    Gielen, J.3    Van Montagu, M.4    Inze, D.5    Boerjan, W.6
  • 22
    • 0001875872 scopus 로고
    • Purification, characterization, and cloning of cinnamyl alcohol dehydrogenase in loblolly pine (Pinus taeda L.)
    • O'Malley, D. M., Porter, S. & Sederoff, R. R. (1992) Purification, characterization, and cloning of cinnamyl alcohol dehydrogenase in loblolly pine (Pinus taeda L.), Plant Physiol. 98, 1364-1371.
    • (1992) Plant Physiol. , vol.98 , pp. 1364-1371
    • O'Malley, D.M.1    Porter, S.2    Sederoff, R.R.3
  • 23
    • 0028980938 scopus 로고
    • Site-directed mutagenesis of a serine residue in cinnamyl alcohol dehydrogenase, a plant NADPH-dependent dehydrogenase, affects the specificity for the coenzyme
    • Lauvergeat, V., Kennedy, K., Feuillet, C., McKie, J. H., Gorrichon, L., Baltas, M., Boudet, A. M., Grima-Pettenati, J. & Douglas, K. T. (1995) Site-directed mutagenesis of a serine residue in cinnamyl alcohol dehydrogenase, a plant NADPH-dependent dehydrogenase, affects the specificity for the coenzyme, Biochemistry 34, 12426-12434.
    • (1995) Biochemistry , vol.34 , pp. 12426-12434
    • Lauvergeat, V.1    Kennedy, K.2    Feuillet, C.3    McKie, J.H.4    Gorrichon, L.5    Baltas, M.6    Boudet, A.M.7    Grima-Pettenati, J.8    Douglas, K.T.9
  • 24
    • 9844229689 scopus 로고
    • Springer Verlag. Berlin Heidelberg New York
    • Lasch, J. (1987) Enzymkinetik, pp. 60-61, Springer Verlag. Berlin Heidelberg New York.
    • (1987) Enzymkinetik , pp. 60-61
    • Lasch, J.1
  • 25
    • 0014844019 scopus 로고
    • The influence of high substrate concentrations on microbial kinetics
    • Edwards, V. H. (1970) The influence of high substrate concentrations on microbial kinetics, Biotechnol. Bioeng. 12, 679-712.
    • (1970) Biotechnol. Bioeng. , vol.12 , pp. 679-712
    • Edwards, V.H.1
  • 26
    • 0018381417 scopus 로고
    • Human liver π-alcohol dehydrogenase: Kinetic and molecular properties
    • Bosron, W. F., Li, T-K., Dafeldecker, W. P. & Vallee, B. L. (1979) Human liver π-alcohol dehydrogenase: kinetic and molecular properties, Biochemistry 18, 1101-1105.
    • (1979) Biochemistry , vol.18 , pp. 1101-1105
    • Bosron, W.F.1    Li, T.-K.2    Dafeldecker, W.P.3    Vallee, B.L.4
  • 27
    • 0028314451 scopus 로고
    • Purification and characterization of a novel carbonyl reductase isolated from Rhodococcus erythropolis
    • Zelinski, T., Peters, J. & Kula, M-R. (1994) Purification and characterization of a novel carbonyl reductase isolated from Rhodococcus erythropolis, J. Biotechnol. 33, 283-292.
    • (1994) J. Biotechnol. , vol.33 , pp. 283-292
    • Zelinski, T.1    Peters, J.2    Kula, M.-R.3
  • 28
    • 0030045445 scopus 로고    scopus 로고
    • Effect of culture conditions on the aldehyde dehydrogenase activity of Acetobacter aceti cytoplasmatic extracts
    • Blandino, A., Caro, I. & Cantero, D. (1996) Effect of culture conditions on the aldehyde dehydrogenase activity of Acetobacter aceti cytoplasmatic extracts, Biotechnol. Lett. 18, 63-68.
    • (1996) Biotechnol. Lett. , vol.18 , pp. 63-68
    • Blandino, A.1    Caro, I.2    Cantero, D.3
  • 29
    • 0030032199 scopus 로고    scopus 로고
    • A second molybdoprotein aldehyde dehydrogenase from Amycolatopsis methanolica NCIB 11946
    • Kim, S. W., Luykx, D. M., de Vries, S. & Duine, J. A. (1996) A second molybdoprotein aldehyde dehydrogenase from Amycolatopsis methanolica NCIB 11946, Arch. Biochem. Biophys. 325, 1-7.
    • (1996) Arch. Biochem. Biophys. , vol.325 , pp. 1-7
    • Kim, S.W.1    Luykx, D.M.2    De Vries, S.3    Duine, J.A.4
  • 30
    • 0022497812 scopus 로고
    • Glucose-fructose oxidoreductase, a new enzyme isolated from Zymomonas mobilis that is responsible for sorbitol production
    • Zachariou, M. & Scopes, R. K. (1986) Glucose-fructose oxidoreductase, a new enzyme isolated from Zymomonas mobilis that is responsible for sorbitol production, J. Bacteriol. 167, 863-869.
    • (1986) J. Bacteriol. , vol.167 , pp. 863-869
    • Zachariou, M.1    Scopes, R.K.2
  • 31
    • 0026730941 scopus 로고
    • Cloning, expression, and sequence analysis of the Bacillus methanolicus C1 methanol dehydrogenase gene
    • De Vries, G. E., Arfman, N., Terpstra, P. & Dijkhuizen, L. (1992) Cloning, expression, and sequence analysis of the Bacillus methanolicus C1 methanol dehydrogenase gene, J. Bacteriol. 174, 5346-5353.
    • (1992) J. Bacteriol. , vol.174 , pp. 5346-5353
    • De Vries, G.E.1    Arfman, N.2    Terpstra, P.3    Dijkhuizen, L.4
  • 32
    • 0025844949 scopus 로고
    • Electron microscopic analysis and biochemical characterization of a novel methanol dehydrogenase from the thermotolerant Bacillus sp. C1
    • Vonck, J., Arfman, N., De Vries, G. E., Van Beeumen, J., Van Bruggen, E. F. J. & Dijkhuizen, L. (1991) Electron microscopic analysis and biochemical characterization of a novel methanol dehydrogenase from the thermotolerant Bacillus sp. C1, J. Biol. Chem. 266, 3949-3954.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3949-3954
    • Vonck, J.1    Arfman, N.2    De Vries, G.E.3    Van Beeumen, J.4    Van Bruggen, E.F.J.5    Dijkhuizen, L.6
  • 33
    • 0021771171 scopus 로고
    • NAD-dependent. PQQ-containing methanol dehydrogenase: A bacterial dehydrogenase multienzyme complex
    • Duine, J. A., Frank, J. & Berkhout, M. P. J. (1984) NAD-dependent. PQQ-containing methanol dehydrogenase: a bacterial dehydrogenase multienzyme complex, FEBS Lett. 168, 217-221.
    • (1984) FEBS Lett. , vol.168 , pp. 217-221
    • Duine, J.A.1    Frank, J.2    Berkhout, M.P.J.3


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