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Volumn 34, Issue 6, 1997, Pages 843-854

Maize glutathione-dependent formaldehyde dehydrogenase cDNA: A novel plant gene of detoxification

Author keywords

Alcohol dehydrogenase; Enzyme evolution; Formaldehyde detoxification; Glutathione dependent formaldehyde dehydrogenase; Heterologous expression

Indexed keywords

ALCOHOL DEHYDROGENASE; ALDEHYDE DEHYDROGENASE; COMPLEMENTARY DNA; FORMALDEHYDE; FORMALDEHYDE DEHYDROGENASE (GLUTATHIONE); GLUTATHIONE; NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 0031214706     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005872222490     Document Type: Article
Times cited : (35)

References (51)
  • 3
    • 0029977557 scopus 로고    scopus 로고
    • Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides
    • Barber RD, Rott MA, Donohue TJ: Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides. J Bact 178: 1386-1393 (1996).
    • (1996) J Bact , vol.178 , pp. 1386-1393
    • Barber, R.D.1    Rott, M.A.2    Donohue, T.J.3
  • 6
    • 0026778829 scopus 로고
    • 'Enzymogenesis': Classical liver alcohol dehydrogenase originate from the glutathione-dependent formaldehyde dehydrogenase line
    • Danielsson O, Jörnvall H: 'Enzymogenesis': classical liver alcohol dehydrogenase originate from the glutathione-dependent formaldehyde dehydrogenase line. Proc Natl Acad Sci USA 89: 9247-9251 (1992).
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9247-9251
    • Danielsson, O.1    Jörnvall, H.2
  • 8
    • 0000026219 scopus 로고
    • Plant DNA miniprep and microprep: Versions 2.1-2.3
    • Freeling M, Walbot V (eds) Springer-Verlag, New York
    • Dellaporta S: Plant DNA miniprep and microprep: versions 2.1-2.3. In: Freeling M, Walbot V (eds) The Maize Handbook, pp. 522-525. Springer-Verlag, New York (1994).
    • (1994) The Maize Handbook , pp. 522-525
    • Dellaporta, S.1
  • 10
    • 0017259111 scopus 로고
    • Structural comparisons of mammalian, yeast and bacillar alcohol dehydrogenases
    • Eklund H, Bränden C-I, Jörnvall H: Structural comparisons of mammalian, yeast and bacillar alcohol dehydrogenases. J Mol Biol 102: 61-73 (1976).
    • (1976) J Mol Biol , vol.102 , pp. 61-73
    • Eklund, H.1    Bränden, C.-I.2    Jörnvall, H.3
  • 14
    • 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, Höög J-O, Holmquist B, Estonius M, Jörnvall H, Vallee BL: 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).
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2491-2494
    • Engeland, K.1    Höög, J.-O.2    Holmquist, B.3    Estonius, M.4    Jörnvall, H.5    Vallee, B.L.6
  • 16
    • 0028641612 scopus 로고
    • Residues specific for class III alcohol dehydrogenase. Site-directed mutagenesis of the human enzyme
    • Estonius M, Höög J-O, Danielsson O, Jörnvall H: Residues specific for class III alcohol dehydrogenase. Site-directed mutagenesis of the human enzyme. Biochemistry 33: 15080-15085 (1994).
    • (1994) Biochemistry , vol.33 , pp. 15080-15085
    • Estonius, M.1    Höög, J.-O.2    Danielsson, O.3    Jörnvall, H.4
  • 17
    • 0029127532 scopus 로고
    • Class III alcohol dehydrogenase from Saccharomyces cerevisiae: Structural and enzymatic features differ toward the human/mammalian forms in a manner consistent with functional needs in formaldehyde detoxication
    • Fernández MR, Biosca JA, Norin A, Jörnvall H, Parés X: Class III alcohol dehydrogenase from Saccharomyces cerevisiae: structural and enzymatic features differ toward the human/mammalian forms in a manner consistent with functional needs in formaldehyde detoxication. FEBS Lett 370: 23-26 (1995).
    • (1995) FEBS Lett , vol.370 , pp. 23-26
    • Fernández, M.R.1    Biosca, J.A.2    Norin, A.3    Jörnvall, H.4    Parés, X.5
  • 18
    • 0027326638 scopus 로고
    • Cephalopod alcohol dehydrogenase: Purification and enzymatic characterization
    • Fernández MR, Jörnvall H, Moreno A, Kaiser R, Parés X: Cephalopod alcohol dehydrogenase: purification and enzymatic characterization. FEBS Lett 328: 235-238 (1993).
    • (1993) FEBS Lett , vol.328 , pp. 235-238
    • Fernández, M.R.1    Jörnvall, H.2    Moreno, A.3    Kaiser, R.4    Parés, X.5
  • 19
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
    • Frohman MA, Dush MK, Martin GR: Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proc Natl Acad Sci USA 85: 8998-9002 (1988).
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 20
    • 0028518756 scopus 로고
    • The reduced stability of a plant alcohol dehydrogenase is due to the substitution of serine for a highly conserved phenylalanine residue
    • Garvin DF, Weeden NF, Doyle JJ: The reduced stability of a plant alcohol dehydrogenase is due to the substitution of serine for a highly conserved phenylalanine residue. Plant Mol Biol 26: 643-655 (1994).
    • (1994) Plant Mol Biol , vol.26 , pp. 643-655
    • Garvin, D.F.1    Weeden, N.F.2    Doyle, J.J.3
  • 22
    • 0027995579 scopus 로고
    • Detoxification of formaldehyde by the spider plant (Chlorophytum comosum L.) and by soybean (Glycine max L.) cell-suspension cultures
    • Giese M, Bauer-Doranth U, Langebartels C, Sandermann H Jr.: Detoxification of formaldehyde by the spider plant (Chlorophytum comosum L.) and by soybean (Glycine max L.) cell-suspension cultures. Plant Physiol 104: 1301-1309 (1994).
    • (1994) Plant Physiol , vol.104 , pp. 1301-1309
    • Giese, M.1    Bauer-Doranth, U.2    Langebartels, C.3    Sandermann Jr., H.4
  • 23
    • 0029042619 scopus 로고
    • Caenorhabditis elegans contains genes encoding two new members of the Zn-containing alcohol dehydrogenase family
    • Glasner JD, Kocher TD, Collins JJ: Caenorhabditis elegans contains genes encoding two new members of the Zn-containing alcohol dehydrogenase family. J Mol Evol 41: 46-53 (1995).
    • (1995) J Mol Evol , vol.41 , pp. 46-53
    • Glasner, J.D.1    Kocher, T.D.2    Collins, J.J.3
  • 24
    • 0024440560 scopus 로고
    • Molecular characterization of the two genes SNQ and SFA that confer hyperresistance to 4-nitroquinoline-N-oxide and formaldehyde in Saccharomyces cerevisiae
    • Gömpel-Klein P, Mack M, Brendel M: Molecular characterization of the two genes SNQ and SFA that confer hyperresistance to 4-nitroquinoline-N-oxide and formaldehyde in Saccharomyces cerevisiae. Curr Genet 16: 65-74 (1989).
    • (1989) Curr Genet , vol.16 , pp. 65-74
    • Gömpel-Klein, P.1    Mack, M.2    Brendel, M.3
  • 25
    • 0000980362 scopus 로고
    • Conservation and duplication of isozymes in plants
    • Gotttlieb LD: Conservation and duplication of isozymes in plants. Science 216: 373-380 (1982).
    • (1982) Science , vol.216 , pp. 373-380
    • Gotttlieb, L.D.1
  • 26
    • 0026512376 scopus 로고
    • Purification, characterization, and partial sequence of the glutathione-dependent formaldehyde dehydrogenase from Escherichia coli: A class III alcohol dehydrogenase
    • Gutheil WG, Holmquist B, Vallee BL: Purification, characterization, and partial sequence of the glutathione-dependent formaldehyde dehydrogenase from Escherichia coli: a class III alcohol dehydrogenase. Biochemistry 31: 475-481 (1992).
    • (1992) Biochemistry , vol.31 , pp. 475-481
    • Gutheil, W.G.1    Holmquist, B.2    Vallee, B.L.3
  • 28
    • 0028809661 scopus 로고
    • Alcohol dehydrogenase of class III: Consistent patterns of structural and functional conservation in relation to class I and other proteins
    • Hjelmqvist L, Shafquat J, Rehman SA, Jörnvall H: Alcohol dehydrogenase of class III: consistent patterns of structural and functional conservation in relation to class I and other proteins. FEBS Lett 373: 212-216 (1995).
    • (1995) FEBS Lett , vol.373 , pp. 212-216
    • Hjelmqvist, L.1    Shafquat, J.2    Rehman, S.A.3    Jörnvall, H.4
  • 29
    • 0027162927 scopus 로고
    • Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase
    • Holmquist B, Moulis J-M, Engeland K, Vallee BL: Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase. Biochemistry 32: 5139-5144 (1993).
    • (1993) Biochemistry , vol.32 , pp. 5139-5144
    • Holmquist, B.1    Moulis, J.-M.2    Engeland, K.3    Vallee, B.L.4
  • 30
    • 0028003547 scopus 로고
    • Messenger RNA 3′ end formation in plants
    • Hunt AG: Messenger RNA 3′ end formation in plants. Annu Rev Plant Phys Plant Mol Biol 45: 47-60 (1994).
    • (1994) Annu Rev Plant Phys Plant Mol Biol , vol.45 , pp. 47-60
    • Hunt, A.G.1
  • 31
    • 0026446802 scopus 로고
    • Cloning and characterization of the ADH5 gene encoding human alcohol dehydrogenase 5, formaldehyde dehydrogenase
    • Hur M-W, Edenberg HJ: Cloning and characterization of the ADH5 gene encoding human alcohol dehydrogenase 5, formaldehyde dehydrogenase. Gene 121: 305-311 (1992).
    • (1992) Gene , vol.121 , pp. 305-311
    • Hur, M.-W.1    Edenberg, H.J.2
  • 32
    • 0028999761 scopus 로고
    • Nomenclature of alcohol dehydrogenases
    • Jörnvall H, Höög J-O: Nomenclature of alcohol dehydrogenases. Alcohol Alcoholism 30: 153-161 (1995).
    • (1995) Alcohol Alcoholism , vol.30 , pp. 153-161
    • Jörnvall, H.1    Höög, J.-O.2
  • 33
    • 0027489769 scopus 로고
    • Origin of the human alcohol dehydrogenase system: Implications from the structure and properties of the octopus protein
    • Kaiser R, Fernández MR, Parés X, Jörnvall H: Origin of the human alcohol dehydrogenase system: Implications from the structure and properties of the octopus protein. Proc Natl Acad Sci USA 90: 11222-11226 (1993).
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11222-11226
    • Kaiser, R.1    Fernández, M.R.2    Parés, X.3    Jörnvall, H.4
  • 35
    • 0023047634 scopus 로고
    • 13C NMR spectroscopy of S-(hydroxymethyl) glutathione as a transient intracellular intermediate
    • 13C NMR spectroscopy of S-(hydroxymethyl) glutathione as a transient intracellular intermediate. Biochemistry 25: 4504-4507 (1986).
    • (1986) Biochemistry , vol.25 , pp. 4504-4507
    • Mason, R.P.1    Sanders, J.K.M.2    Crawford, A.3    Hunter, B.K.4
  • 36
    • 1842339228 scopus 로고
    • Purification of maize alcohol dehydrogenase and competitive inhibition by pyrazoles
    • Pryor A, Huppatz JL: Purification of maize alcohol dehydrogenase and competitive inhibition by pyrazoles. Biochem Int 4: 431-438 (1982).
    • (1982) Biochem Int , vol.4 , pp. 431-438
    • Pryor, A.1    Huppatz, J.L.2
  • 37
    • 0028872476 scopus 로고
    • Isolation, sequencing, and mutagenesis of the gene encoding NAD-and glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growth
    • Ras J, Van Ophem PW, Reijenders WNM, Van Spanning RJM, Duine JA, Stouthamer AH, Harms N: Isolation, sequencing, and mutagenesis of the gene encoding NAD-and glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growth. J Bact 177: 247-251 (1994).
    • (1994) J Bact , vol.177 , pp. 247-251
    • Ras, J.1    Van Ophem, P.W.2    Reijenders, W.N.M.3    Van Spanning, R.J.M.4    Duine, J.A.5    Stouthamer, A.H.6    Harms, N.7
  • 38
    • 0346981731 scopus 로고
    • Two alleles of maize alcohol dehydrogenase 1 have 3′ structural and poly(A) addition polymorphisms
    • Sachs MM, Dennis ES, Gerlach WL, Peacock WJ: Two alleles of maize alcohol dehydrogenase 1 have 3′ structural and poly(A) addition polymorphisms. Genetics 113: 449-467 (1986).
    • (1986) Genetics , vol.113 , pp. 449-467
    • Sachs, M.M.1    Dennis, E.S.2    Gerlach, W.L.3    Peacock, W.J.4
  • 39
    • 0018869288 scopus 로고
    • The anaerobic proteins of maize
    • Sachs MM, Freeling M, Okimoto R: The anaerobic proteins of maize. Cell 20: 761-767 (1980).
    • (1980) Cell , vol.20 , pp. 761-767
    • Sachs, M.M.1    Freeling, M.2    Okimoto, R.3
  • 41
    • 0028020325 scopus 로고
    • Higher plant metabolism of xenobiotics: The 'green liver' concept
    • Sandermann H Jr.: Higher plant metabolism of xenobiotics: the 'green liver' concept. Pharmacogenetics 4: 225-241 (1994).
    • (1994) Pharmacogenetics , vol.4 , pp. 225-241
    • Sandermann Jr., H.1
  • 42
    • 0026460717 scopus 로고
    • Cloning and analysis of a Candida maltosa gene which confers resistance to formaldehyde in Saccharomyces cerivisiae
    • Sasnauskas K, Jomantiene R, Januska A, Lebediene E, Lebedys J, Janulaitis A: Cloning and analysis of a Candida maltosa gene which confers resistance to formaldehyde in Saccharomyces cerivisiae. Gene 122: 207-211 (1992).
    • (1992) Gene , vol.122 , pp. 207-211
    • Sasnauskas, K.1    Jomantiene, R.2    Januska, A.3    Lebediene, E.4    Lebedys, J.5    Janulaitis, A.6
  • 43
    • 0018785977 scopus 로고
    • Concomitant induction of phenylalanine ammonia-lyase and flavanone synthase mRNAs in irradiated plant cells
    • Schröder J, Kreuzaler F, Schäfer E, Hahlbrock K: Concomitant induction of phenylalanine ammonia-lyase and flavanone synthase mRNAs in irradiated plant cells. J Biol Chem 254: 57-65 (1979).
    • (1979) J Biol Chem , vol.254 , pp. 57-65
    • Schröder, J.1    Kreuzaler, F.2    Schäfer, E.3    Hahlbrock, K.4
  • 44
    • 0029941709 scopus 로고    scopus 로고
    • Pea formaldehyde-active class III alcohol dehydrogenase: Common derivation of the plant and animal forms but not of the corresponding ethanol-active forms (classes I and P)
    • Shafqat J, El-Ahmad M, Danielsson O, Martínez MC, Persson B, Parés X, Jörnvall H: Pea formaldehyde-active class III alcohol dehydrogenase: common derivation of the plant and animal forms but not of the corresponding ethanol-active forms (classes I and P). Proc Natl Acad Sci USA 93: 5595-5599 (1996).
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5595-5599
    • Shafqat, J.1    El-Ahmad, M.2    Danielsson, O.3    Martínez, M.C.4    Persson, B.5    Parés, X.6    Jörnvall, H.7
  • 45
    • 0000778417 scopus 로고
    • Formaldehyde dehydrogenase, a glutathione-dependent enzyme system
    • Strittmatter P, Ball EG: Formaldehyde dehydrogenase, a glutathione-dependent enzyme system. J Biol Chem 213: 445-461 (1955).
    • (1955) J Biol Chem , vol.213 , pp. 445-461
    • Strittmatter, P.1    Ball, E.G.2
  • 46
    • 0027968068 scopus 로고
    • Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ: Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nuc Acids Res 22: 4673-4680 (1994).
    • (1994) Nuc Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3    Clustal, W.4
  • 47
    • 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, Koivusalo M: 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).
    • (1979) Arch Biochem Biophys , vol.196 , pp. 33-45
    • Uotila, L.1    Koivusalo, M.2
  • 49
    • 0000221995 scopus 로고
    • Glutathione-dependent oxidoreductases: Formaldehyde dehydrogenase
    • Dolphin D, Poulson R, Avramovic O (eds) John Wiley, New York
    • Uotila L, Koivusalo M: Glutathione-dependent oxidoreductases: formaldehyde dehydrogenase. In: Dolphin D, Poulson R, Avramovic O (eds) Coenzymes and Cofactors, Vol. III. Glutathione, pp. 517-551. John Wiley, New York (1989).
    • (1989) Coenzymes and Cofactors, Vol. III. Glutathione , vol.3 , pp. 517-551
    • Uotila, L.1    Koivusalo, M.2
  • 50
    • 0027463082 scopus 로고
    • Molecular structure and genetic regulation of SFA, a gene responsible for resistance to formaldehyde in Saccharomyces cerevisiae, and characterization of its gene product
    • Wehner EP, Rao E, Brendel M: Molecular structure and genetic regulation of SFA, a gene responsible for resistance to formaldehyde in Saccharomyces cerevisiae, and characterization of its gene product. Mol Gen Genet 237: 351-358 (1993).
    • (1993) Mol Gen Genet , vol.237 , pp. 351-358
    • Wehner, E.P.1    Rao, E.2    Brendel, M.3
  • 51
    • 0027428004 scopus 로고
    • Molecular phylogeny and evolutionary rates of alcohol dehydrogenases in vertebrates and plants
    • Yokoyama S, Harry DE: Molecular phylogeny and evolutionary rates of alcohol dehydrogenases in vertebrates and plants. Mol Biol Evol 10: 1215-1226 (1993).
    • (1993) Mol Biol Evol , vol.10 , pp. 1215-1226
    • Yokoyama, S.1    Harry, D.E.2


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