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Volumn 178, Issue 5, 1996, Pages 1386-1393

Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides

Author keywords

[No Author keywords available]

Indexed keywords

FORMALDEHYDE DEHYDROGENASE; GLUTATHIONE;

EID: 0029977557     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.5.1386-1393.1996     Document Type: Article
Times cited : (45)

References (47)
  • 1
    • 0003191832 scopus 로고
    • BRL pUC host: Escherichia coli DH5αTM competent cells
    • Bethesda Research Laboratories. 1986. BRL pUC host: Escherichia coli DH5αTM competent cells Bethesda Res Lab. Focus 8:9-10.
    • (1986) Bethesda Res Lab. Focus , vol.8 , pp. 9-10
  • 3
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J. R., P. Haeberli, and O. Smithies. 1984 A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12:387-395
    • (1984) Nucleic Acids Res , vol.12 , pp. 387-395
    • Devereux, J.R.1    Haeberli, P.2    Smithies, O.3
  • 6
    • 0027478178 scopus 로고
    • Mutation of Arg-115 of human class III alcohol dehydrogenase: A binding site required for formaldehyde dehydrogenase activity and fatty acid activation
    • Engeland, K., J. Hoog, B. Holmquist, M. Estonius, H. Jornvall, and B. L. Vallee. 1993. Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation Proc Natl Acad. Sci. USA 90:2491-2494.
    • (1993) Proc Natl Acad. Sci. USA , vol.90 , pp. 2491-2494
    • Engeland, K.1    Hoog, J.2    Holmquist, B.3    Estonius, M.4    Jornvall, H.5    Vallee, B.L.6
  • 7
    • 0001522673 scopus 로고
    • Starch-gel electrophoresis - Application to the classification of pituitary proteins and polypeptides
    • Ferguson, K. A. 1964. Starch-gel electrophoresis - application to the classification of pituitary proteins and polypeptides. Metabolism 13:985-1002
    • (1964) Metabolism , vol.13 , pp. 985-1002
    • Ferguson, K.A.1
  • 9
    • 0026512376 scopus 로고
    • Purification, characterization, and partial sequence of the glutathione-dependent formaldehyde dehydrogenase from Escherichia coli: A class III alcohol dehydrogenase
    • Gutheil, W. G., B. Holmquist, and B. L. Vallee. 1992. Purification, characterization, and partial sequence of the glutathione-dependent formaldehyde dehydrogenase from Escherichia coli: a class III alcohol dehydrogenase Biochemistry 31:475-481.
    • (1992) Biochemistry , vol.31 , pp. 475-481
    • Gutheil, W.G.1    Holmquist, B.2    Vallee, B.L.3
  • 10
    • 0014310082 scopus 로고
    • Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis
    • Hendrick, J. L., and A. J. Smith. 1968 Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis Arch Biochem Biophys. 126:155-164
    • (1968) Arch Biochem Biophys. , vol.126 , pp. 155-164
    • Hendrick, J.L.1    Smith, A.J.2
  • 11
    • 0027162927 scopus 로고
    • Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase
    • Holmquist, B., J. Moulis, K. Engeland, and B. L. Vallee. 1993. Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase. Biochemistry 32:5139-5144.
    • (1993) Biochemistry , vol.32 , pp. 5139-5144
    • Holmquist, B.1    Moulis, J.2    Engeland, K.3    Vallee, B.L.4
  • 12
    • 0026446802 scopus 로고
    • Cloning and characterization of the ADH5 gene encoding human alcohol dehydrogenase 5, formaldehyde dehydrogenase
    • Hur, M., and H. J. Edenberg. 1992. Cloning and characterization of the ADH5 gene encoding human alcohol dehydrogenase 5, formaldehyde dehydrogenase. Gene 121:305-311.
    • (1992) Gene , vol.121 , pp. 305-311
    • Hur, M.1    Edenberg, H.J.2
  • 13
    • 0023411028 scopus 로고
    • Characteristics of alcohol/polyol dehydrogenases: The zinc-contaimng long-chain alcohol dehydrogenases
    • Jornvall, H., B. Persson, and J. Jeffery. 1987. Characteristics of alcohol/polyol dehydrogenases: the zinc-contaimng long-chain alcohol dehydrogenases. Eur. J. Biochem. 167:195-201.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 195-201
    • Jornvall, H.1    Persson, B.2    Jeffery, J.3
  • 14
    • 0023093115 scopus 로고
    • Characterization of three isoenzymes of rat alcohol dehydrogenase: Tissue distribution and physical and enzymatic properties
    • Julia, P., J. Farres, and X. Pares. 1987. Characterization of three isoenzymes of rat alcohol dehydrogenase: tissue distribution and physical and enzymatic properties. Eur J. Biochem. 162:179-189.
    • (1987) Eur J. Biochem. , vol.162 , pp. 179-189
    • Julia, P.1    Farres, J.2    Pares, X.3
  • 15
    • 0024460552 scopus 로고
    • Characteristics of mammalian class III alcohol dehydrogenases, an enzyme less variable than the traditional liver enzyme class I
    • Kaiser, R., B. Holmquist, B. L. Vallee, and H. Jornvall. 1989. Characteristics of mammalian class III alcohol dehydrogenases, an enzyme less variable than the traditional liver enzyme class I. Biochemistry 28:8432-8438.
    • (1989) Biochemistry , vol.28 , pp. 8432-8438
    • Kaiser, R.1    Holmquist, B.2    Vallee, B.L.3    Jornvall, H.4
  • 16
    • 0025760370 scopus 로고
    • Demonstration of formaldehyde dehydrogenase activity in formaldehyde-resistant Enterobacteriaceae
    • Kaulfers, P., and A. Marquardt. 1991. Demonstration of formaldehyde dehydrogenase activity in formaldehyde-resistant Enterobacteriaceae. FEMS Microbiol. Lett. 79:335-338
    • (1991) FEMS Microbiol. Lett. , vol.79 , pp. 335-338
    • Kaulfers, P.1    Marquardt, A.2
  • 17
    • 0025804146 scopus 로고
    • Glutathione-dependent formaldehyde dehydrogenase (EC 1.2.1.1): Evidence for the identity with class III alcohol dehydrogenase
    • H Weiner, B. Wermuth, and D W. Crabb (ed). Plenum Press, New York
    • Koivusalo, M., and L. Uotila. 1990 Glutathione-dependent formaldehyde dehydrogenase (EC 1.2.1.1): evidence for the identity with class III alcohol dehydrogenase, p. 305-313. In H Weiner, B. Wermuth, and D W. Crabb (ed). Enzymology and molecular biology of carbonyl metabolism 3. Plenum Press, New York.
    • (1990) Enzymology and Molecular Biology of Carbonyl Metabolism 3 , pp. 305-313
    • Koivusalo, M.1    Uotila, L.2
  • 18
    • 0001225246 scopus 로고
    • The oxidative demethylation of monomethyl-L-amino acids
    • Ling, K., and T. Tung. 1948. The oxidative demethylation of monomethyl-L-amino acids. J. Biol Chem. 174:643-645.
    • (1948) J. Biol Chem. , vol.174 , pp. 643-645
    • Ling, K.1    Tung, T.2
  • 20
    • 0017879080 scopus 로고
    • Membrane-bound, pyrimidine nucleotide-independent L-lactate dehydrogenase of Rhodopseudomonas sphaeroides
    • Markwell, J. P., and J. Lascelles. 1978. Membrane-bound, pyrimidine nucleotide-independent L-lactate dehydrogenase of Rhodopseudomonas sphaeroides. J. Bacteriol. 133:593-600.
    • (1978) J. Bacteriol. , vol.133 , pp. 593-600
    • Markwell, J.P.1    Lascelles, J.2
  • 21
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell, M. A. K., S. M. Haas, L. L. Bieber, and N. E. Tolbert. 1978. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples Anal. Biochem. 87:206-210.
    • (1978) Anal. Biochem. , vol.87 , pp. 206-210
    • Markwell, M.A.K.1    Haas, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 22
    • 0023047634 scopus 로고
    • 13C NMR spectroscopy of S-(hydroxy-methyl)glutathione as a transient intracellular intermediate
    • 13C NMR spectroscopy of S-(hydroxy-methyl)glutathione as a transient intracellular intermediate. Biochemistry 25:4504-4507.
    • (1986) Biochemistry , vol.25 , pp. 4504-4507
    • Mason, R.P.1    Sanders, J.K.M.2
  • 23
    • 0018562382 scopus 로고
    • A multipurpose cloning system based on single stranded DNA bacteriophage M13
    • Messing, J. 1979. A multipurpose cloning system based on single stranded DNA bacteriophage M13. Recomb DNA Tech. Bull. 2:43-48.
    • (1979) Recomb DNA Tech. Bull. , vol.2 , pp. 43-48
    • Messing, J.1
  • 24
    • 0000134772 scopus 로고
    • 1 complex to photosynthetic reaction center complexes
    • R. E Blankenship, M. T. Madigan, and C. E Bauer (ed.), Kluwer Academic Publishers, The Netherlands
    • 1 complex to photosynthetic reaction center complexes, p. 725-745. In R. E Blankenship, M. T. Madigan, and C. E Bauer (ed.), Anoxygenic photosynthetic bacteria Kluwer Academic Publishers, The Netherlands
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 725-745
    • Meyer, T.E.1    Donohue, T.J.2
  • 25
    • 0021103537 scopus 로고
    • Microbial oxidation of methanol: Purification of formaldehyde dehydrogenase from Pichia sp. NRRL-Y-11328
    • Patel, R. N., C. T. Hou, and P. Derelanko. 1983 Microbial oxidation of methanol: purification of formaldehyde dehydrogenase from Pichia sp. NRRL-Y-11328. Arch. Biochem. Biophys. 221:135-142.
    • (1983) Arch. Biochem. Biophys. , vol.221 , pp. 135-142
    • Patel, R.N.1    Hou, C.T.2    Derelanko, P.3
  • 26
    • 0021592032 scopus 로고
    • In vitro insertional mutagenesis with a selectable DNA fragment
    • Prentki, P., and H. M. Krisch. 1984. In vitro insertional mutagenesis with a selectable DNA fragment. Gene 29:303-313.
    • (1984) Gene , vol.29 , pp. 303-313
    • Prentki, P.1    Krisch, H.M.2
  • 27
    • 0027991575 scopus 로고
    • Crystallization and crystallographic investigations of cod alcohol dehydrogenase class I and class III enzymes
    • Ramaswamy, S., M. el-Ahmad, O. Danielsson, H. Jornvall, and H. Eklund. 1994. Crystallization and crystallographic investigations of cod alcohol dehydrogenase class I and class III enzymes FEBS Lett. 350:122-124.
    • (1994) FEBS Lett. , vol.350 , pp. 122-124
    • Ramaswamy, S.1    El-Ahmad, M.2    Danielsson, O.3    Jornvall, H.4    Eklund, H.5
  • 28
    • 0028872476 scopus 로고
    • Isolation, sequencing, and mutagenesis of the gene encoding NAD- and glutathione-dependent formaldehyde dehydrogenase (CD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growth
    • Ras, J., P. W. Van Ophem, W. N. M. Reijnders, R. J. M. Van Spanning, J. A. Duine, A. H. Stouthammer, and N. Harms. 1995 Isolation, sequencing, and mutagenesis of the gene encoding NAD- and glutathione-dependent formaldehyde dehydrogenase (CD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growth J. Bacteriol. 177: 247-251.
    • (1995) J. Bacteriol. , vol.177 , pp. 247-251
    • Ras, J.1    Van Ophem, P.W.2    Reijnders, W.N.M.3    Van Spanning, R.J.M.4    Duine, J.A.5    Stouthammer, A.H.6    Harms, N.7
  • 29
  • 32
    • 0017195101 scopus 로고
    • Metabolism of methanol by Rhodopseudomonas acidophila
    • Sahm, H., R. B. Cox, and J. R. Quayle. 1976. Metabolism of methanol by Rhodopseudomonas acidophila. J Gen. Microbiol. 94:313-322
    • (1976) J Gen. Microbiol. , vol.94 , pp. 313-322
    • Sahm, H.1    Cox, R.B.2    Quayle, J.R.3
  • 33
    • 0026460717 scopus 로고
    • Cloning and analysis of Candida maltosa gene which confers resistance to formaldehyde in Saccharomyces cerevisiae
    • Sasnauskas, K., R. Jomantiene, A. Januska, E. Levediene, J. Lebedys, and A. Janulaitis. 1992. Cloning and analysis of Candida maltosa gene which confers resistance to formaldehyde in Saccharomyces cerevisiae. Gene 122:207-211.
    • (1992) Gene , vol.122 , pp. 207-211
    • Sasnauskas, K.1    Jomantiene, R.2    Januska, A.3    Levediene, E.4    Lebedys, J.5    Janulaitis, A.6
  • 34
    • 0028357193 scopus 로고
    • The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene
    • Satre, M. A., M. Zgombic-Knight, and G. Duester. 1994. The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene J. Biol. Chem. 269:15606-15612.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15606-15612
    • Satre, M.A.1    Zgombic-Knight, M.2    Duester, G.3
  • 36
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram negative bacteria
    • Simon, R., U. Priefer, and A. Puhler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram negative bacteria. Bio/Technology 1:784-791
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 37
    • 72849182812 scopus 로고
    • A requirement for sodium in the growth of Rhodopseudomonas sphaeroides
    • Sistrom, W. R. 1960 A requirement for sodium in the growth of Rhodopseudomonas sphaeroides J Gen. Microbiol 22:778-785.
    • (1960) J Gen. Microbiol , vol.22 , pp. 778-785
    • Sistrom, W.R.1
  • 38
    • 0022350092 scopus 로고
    • Intracellular localization of phospholipid transfer activity in Rhodopseudomonas sphaeroides and a possible role in membrane biogenesis
    • Tai, S. P., and S. Kaplan. 1985. Intracellular localization of phospholipid transfer activity in Rhodopseudomonas sphaeroides and a possible role in membrane biogenesis. J. Bacteriol. 164:181-186.
    • (1985) J. Bacteriol. , vol.164 , pp. 181-186
    • Tai, S.P.1    Kaplan, S.2
  • 39
    • 0018503022 scopus 로고
    • Purification of formaldehyde and formate dehydrogenases from pea seeds by affinity chromatography and S-formylglutathione as the intermediate of formaldehyde metabolism
    • Uotila, L., and M. Koivusalo. 1979. Purification of formaldehyde and formate dehydrogenases from pea seeds by affinity chromatography and S-formylglutathione as the intermediate of formaldehyde metabolism. Arch. Biochem. Biophys. 196:33-45
    • (1979) Arch. Biochem. Biophys. , vol.196 , pp. 33-45
    • Uotila, L.1    Koivusalo, M.2
  • 40
  • 41
    • 0018378125 scopus 로고
    • A steady-state kinetic model for formaldehyde dehydrogenase from human liver
    • Uotila, L., and B. Mannervik. 1979. A steady-state kinetic model for formaldehyde dehydrogenase from human liver Biochem. J. 177:869-878.
    • (1979) Biochem. J. , vol.177 , pp. 869-878
    • Uotila, L.1    Mannervik, B.2
  • 42
    • 0019836617 scopus 로고
    • Electrophoretic comparison of enzymes in gram negative methanol utilizing bacteria
    • Urakami, T., and K. Komagata. 1981. Electrophoretic comparison of enzymes in gram negative methanol utilizing bacteria. J. Gen. Appl Microbiol. 27:381-403.
    • (1981) J. Gen. Appl Microbiol. , vol.27 , pp. 381-403
    • Urakami, T.1    Komagata, K.2
  • 43
    • 0021757678 scopus 로고
    • Physical and enzymatic properties of a class III isozyme of human liver alcohol dehydrogenase: χ-ADH
    • Wagner, F. W., X. Pares, B. Holmquist, and B. L. Vallee. 1984. Physical and enzymatic properties of a class III isozyme of human liver alcohol dehydrogenase: χ-ADH. Biochemistry 23:2193-2199.
    • (1984) Biochemistry , vol.23 , pp. 2193-2199
    • Wagner, F.W.1    Pares, X.2    Holmquist, B.3    Vallee, B.L.4
  • 44
    • 0022406342 scopus 로고
    • Methanol dissimilation in Xanthobacter H4-14: Activities, induction and comparison to Pseudomonas AMI and Paracoccus denitrificans
    • Weaver, C. A., and M. E. Lidstrom. 1985. Methanol dissimilation in Xanthobacter H4-14: activities, induction and comparison to Pseudomonas AMI and Paracoccus denitrificans. J. Gen. Microbiol 131:2183-2197.
    • (1985) J. Gen. Microbiol , vol.131 , pp. 2183-2197
    • Weaver, C.A.1    Lidstrom, M.E.2
  • 45
    • 0027463082 scopus 로고
    • Molecular structure and genetic regulation of SFA, a gene responsible for resistance to formaldehyde in Saccharomyces cerevisiae, and characterization of its protein product
    • Wehner, E. P., E. Rao, and M. Brendel. 1993. Molecular structure and genetic regulation of SFA, a gene responsible for resistance to formaldehyde in Saccharomyces cerevisiae, and characterization of its protein product. Mol Gen. Genet. 237:351-358.
    • (1993) Mol Gen. Genet. , vol.237 , pp. 351-358
    • Wehner, E.P.1    Rao, E.2    Brendel, M.3
  • 47
    • 0021813055 scopus 로고
    • Effects of light, oxygen, and substrates on steady-state levels of mRNA coding for ribulose-1,5-bisphosphate carboxylase and light-harvesting and reaction center polypeptides in Rhodopseudomonas sphaeroides
    • Zhu, Y. S., and S. Kaplan. 1985. Effects of light, oxygen, and substrates on steady-state levels of mRNA coding for ribulose-1,5-bisphosphate carboxylase and light-harvesting and reaction center polypeptides in Rhodopseudomonas sphaeroides. J. Bacteriol. 162:925-932.
    • (1985) J. Bacteriol. , vol.162 , pp. 925-932
    • Zhu, Y.S.1    Kaplan, S.2


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