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Volumn 162, Issue 2, 1998, Pages 257-264

Dissimilatory ATP sulfurylase from the hyperthermophilic sulfate reducer Archaeoglobus fulgidus belongs to the group of homo-oligomeric ATP sulfurylases

Author keywords

Adenosine triphosphate sulfurylase; Adenosine 5' phosphosulfate reductase; Archaeoglobus fulgidus; Dissimilatory sulfate reduction; Heterologous expression; Hyperthermophilic archaea

Indexed keywords

OXIDOREDUCTASE; SULFATE ADENYLYLTRANSFERASE;

EID: 0032525257     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(98)00120-7     Document Type: Article
Times cited : (29)

References (28)
  • 1
    • 0002121607 scopus 로고
    • Dissimilatory reduction of sulfur compounds
    • (Zehnder, A.J.B., Ed.) John Wiley, New York
    • LeGall, J. and Fauque, G. (1988) Dissimilatory reduction of sulfur compounds. In: Biology of Anaerobic Microorganisms (Zehnder, A.J.B., Ed.), pp. 587-639. John Wiley, New York.
    • (1988) Biology of Anaerobic Microorganisms , pp. 587-639
    • LeGall, J.1    Fauque, G.2
  • 2
    • 0002739302 scopus 로고    scopus 로고
    • Assimilatory reduction of inorganic sulfate
    • (Cram, W.J. et al., Eds.) Backhuys, Leiden
    • Schwenn, J.D. (1997) Assimilatory reduction of inorganic sulfate. In: Sulphur Metabolism in Higher Plants (Cram, W.J. et al., Eds.), pp. 39-58. Backhuys, Leiden.
    • (1997) Sulphur Metabolism in Higher Plants , pp. 39-58
    • Schwenn, J.D.1
  • 3
    • 0032466668 scopus 로고    scopus 로고
    • Physiology and genetics of sulfur-oxidizing bacteria
    • Friedrich, C.G. (1997) Physiology and genetics of sulfur-oxidizing bacteria. Adv. Microb. Physiol. 39, 235-289.
    • (1997) Adv. Microb. Physiol. , vol.39 , pp. 235-289
    • Friedrich, C.G.1
  • 4
    • 0028674004 scopus 로고
    • Enzymes of dissimilatory sulfide oxidation in phototropic bacteria
    • Dahl, C. and Trüper, H.G. (1994) Enzymes of dissimilatory sulfide oxidation in phototropic bacteria. Methods Enzymol. 243, 400-421.
    • (1994) Methods Enzymol. , vol.243 , pp. 400-421
    • Dahl, C.1    Trüper, H.G.2
  • 5
    • 0023159558 scopus 로고
    • Isolation of extremely thermophilic sulfate reducers: Evidence for a new branch of archaebacteria
    • Stetter, K.O., Lauerer, G., Thomm, M. and Neuner, A. (1987) Isolation of extremely thermophilic sulfate reducers: evidence for a new branch of archaebacteria. Science 236, 822-824.
    • (1987) Science , vol.236 , pp. 822-824
    • Stetter, K.O.1    Lauerer, G.2    Thomm, M.3    Neuner, A.4
  • 6
    • 0025952777 scopus 로고
    • Archaeal phylogeny: Reexamination of the phylogenetic position of Archaeoglobus fulgidus in light of certain composition-induced artifacts
    • Woese, C.R., Achenbach, L., Rouviere, P. and Mandelco, L. (1991) Archaeal phylogeny: reexamination of the phylogenetic position of Archaeoglobus fulgidus in light of certain composition-induced artifacts. Syst. Appl. Microbiol. 14, 364-371.
    • (1991) Syst. Appl. Microbiol. , vol.14 , pp. 364-371
    • Woese, C.R.1    Achenbach, L.2    Rouviere, P.3    Mandelco, L.4
  • 7
    • 0025034584 scopus 로고
    • Purification and characterization of ATP sulfurylase from the extremely thermophilic archaebacterial sulfate-reducer, Archaeoglobus fulgidus
    • Dahl, C., Koch, H.-G., Keuken, O. and Trüper, H.G. (1990) Purification and characterization of ATP sulfurylase from the extremely thermophilic archaebacterial sulfate-reducer, Archaeoglobus fulgidus. FEMS Microbiol. Lett. 67, 27-32.
    • (1990) FEMS Microbiol. Lett. , vol.67 , pp. 27-32
    • Dahl, C.1    Koch, H.-G.2    Keuken, O.3    Trüper, H.G.4
  • 8
    • 0027275049 scopus 로고
    • Dissimilatory sulphite reductase from Archaeoglobus fulgidus: Physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes
    • Dahl, C., Kredich, N.M., Deutzmann, R. and Trüper, H.G. (1993) Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes. J. Gen. Microbiol. 139, 1817-1828.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 1817-1828
    • Dahl, C.1    Kredich, N.M.2    Deutzmann, R.3    Trüper, H.G.4
  • 9
    • 0028284389 scopus 로고
    • Adenylylsulphate reductase from the sulphate-reducing archaeon Archaeoglobus fulgidus: Cloning and characterisation of the genes and comparison of the enzyme with other iron-sulphur flavoproteins
    • Speich, N., Dahl, C., Heisig, P., Klein, A., Lottspeich, F., Stetter, K.O. and Trüper, H.G. (1994) Adenylylsulphate reductase from the sulphate-reducing archaeon Archaeoglobus fulgidus: cloning and characterisation of the genes and comparison of the enzyme with other iron-sulphur flavoproteins. Microbiology 140, 1273-1284.
    • (1994) Microbiology , vol.140 , pp. 1273-1284
    • Speich, N.1    Dahl, C.2    Heisig, P.3    Klein, A.4    Lottspeich, F.5    Stetter, K.O.6    Trüper, H.G.7
  • 10
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus
    • Klenk, H.-P., Clayton, R.A., Tomb, J.-F., White, O., Nelson, K.E., Ketchum, K.A., Dodson, R.J., et al. (1997) The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390, 364-370.
    • (1997) Nature , vol.390 , pp. 364-370
    • Klenk, H.-P.1    Clayton, R.A.2    Tomb, J.-F.3    White, O.4    Nelson, K.E.5    Ketchum, K.A.6    Dodson, R.J.7
  • 11
    • 0001258765 scopus 로고
    • Sulfate activation and transfer
    • Metabolic Pathways (Greenberg, D.M., Ed.) Academic Press, New York
    • De Meio, R.H. (1975) Sulfate activation and transfer. In: Metabolic Pathways, Vol. VII. Metabolism of Sulfur Compound (Greenberg, D.M., Ed.), pp. 287-358. Academic Press, New York.
    • (1975) Metabolism of Sulfur Compound , vol.7 , pp. 287-358
    • De Meio, R.H.1
  • 12
    • 0028672437 scopus 로고
    • Enzymology and molecular biology of sulfate reduction in the extremely thermophilic archaeon Archaeoglobus fulgidus
    • Dahl, C., Speich, N. and Trüper, H.G. (1994) Enzymology and molecular biology of sulfate reduction in the extremely thermophilic archaeon Archaeoglobus fulgidus. Methods Enzymol. 243, 331-349.
    • (1994) Methods Enzymol. , vol.243 , pp. 331-349
    • Dahl, C.1    Speich, N.2    Trüper, H.G.3
  • 13
    • 0023874416 scopus 로고
    • The sulfate activation locus of Escherichia coli K12: Cloning, genetic, and enzymatic characterization
    • Leyh, T.S., Taylor, J.C. and Markham, G.D. (1988) The sulfate activation locus of Escherichia coli K12: cloning, genetic, and enzymatic characterization. J. Biol. Chem. 263, 2409-2416.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2409-2416
    • Leyh, T.S.1    Taylor, J.C.2    Markham, G.D.3
  • 15
    • 77956844355 scopus 로고
    • Archaeal hyperthermophile genes
    • (Kates, M., Kushner, D.J. and Matheson, A.T., Eds.) Elsevier, Amsterdam
    • Dalgaard, J.Z. and Garrett, R.A. (1993) Archaeal hyperthermophile genes. In: The Biochemistry of Archaea (Archaebacteria) (Kates, M., Kushner, D.J. and Matheson, A.T., Eds.), pp. 535-563. Elsevier, Amsterdam.
    • (1993) The Biochemistry of Archaea (Archaebacteria) , pp. 535-563
    • Dalgaard, J.Z.1    Garrett, R.A.2
  • 16
    • 0029864566 scopus 로고    scopus 로고
    • Sequence, expression in Escherichia coli, and analysis of the gene encoding a novel intracellular protease (PfpI) from the hyperthermophilic archaeon Pyrococcus furiosus
    • Halio, S.B., Blumenthals, I.I., Short, S.A., Merrill, B.M. and Kelly, R.M. (1996) Sequence, expression in Escherichia coli, and analysis of the gene encoding a novel intracellular protease (PfpI) from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 178, 2605-2612.
    • (1996) J. Bacteriol. , vol.178 , pp. 2605-2612
    • Halio, S.B.1    Blumenthals, I.I.2    Short, S.A.3    Merrill, B.M.4    Kelly, R.M.5
  • 17
    • 0028978064 scopus 로고
    • Formylmethanofuran: Tetrahydromethanopterin formyltransferase (Ftr) from the hyperthermophilic Methanopyrus kandleri. Cloning, sequencing and functional expression of the ftr gene and one-step purification of the enzyme overproduced in Escherichia coli
    • Shima, S., Weiss, D.S. and Thauer, R.K. (1995) Formylmethanofuran: tetrahydromethanopterin formyltransferase (Ftr) from the hyperthermophilic Methanopyrus kandleri. Cloning, sequencing and functional expression of the ftr gene and one-step purification of the enzyme overproduced in Escherichia coli. Eur. J. Biochem. 230, 906-913.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 906-913
    • Shima, S.1    Weiss, D.S.2    Thauer, R.K.3
  • 18
    • 0030610167 scopus 로고    scopus 로고
    • 10-methylenetetrahydromethanopterin dehydrogenase gene from the hyperthermophilic Methanopyrus kandleri
    • 10-methylenetetrahydromethanopterin dehydrogenase gene from the hyperthermophilic Methanopyrus kandleri. Eur. J. Biochem. 245, 386-391.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 386-391
    • Klein, A.R.1    Thauer, R.K.2
  • 19
    • 0030726657 scopus 로고    scopus 로고
    • Crystal structure of methyl coenzyme M reductase: The key enzyme of biological methane formation
    • Ermler, U., Grabarse, W., Shima, S., Goubeaud, M. and Thauer, R.K. (1997) Crystal structure of methyl coenzyme M reductase: The key enzyme of biological methane formation. Science 278, 1457-1462.
    • (1997) Science , vol.278 , pp. 1457-1462
    • Ermler, U.1    Grabarse, W.2    Shima, S.3    Goubeaud, M.4    Thauer, R.K.5
  • 20
    • 0024234855 scopus 로고
    • Clustal: A package for performing multiple sequence alignment on a microcomputer
    • Higgins, D.G. and Sharp, P.M. (1989) Clustal: a package for performing multiple sequence alignment on a microcomputer. Gene 73, 237-244.
    • (1989) Gene , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 21
    • 0028786032 scopus 로고
    • The isolation and characterization of cDNA encoding the mouse bifunctional ATP sulfurylase-adenosine 5′-phosphosulfate kinase
    • Li, H., Deyrup, A., Mensch, J.R., Domowicz, M., Konstantinidis, A.K. and Schwartz, N.B. (1995) The isolation and characterization of cDNA encoding the mouse bifunctional ATP sulfurylase-adenosine 5′-phosphosulfate kinase. J. Biol. Chem. 270, 29453-29459.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29453-29459
    • Li, H.1    Deyrup, A.2    Mensch, J.R.3    Domowicz, M.4    Konstantinidis, A.K.5    Schwartz, N.B.6
  • 22
    • 0028050646 scopus 로고
    • Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum: Identification of a likely allosteric domain
    • Foster, B.A., Thomas, S.M., Mahr, J.A., Renosto, F., Patel, H.C. and Segel, I.H. (1994) Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum: Identification of a likely allosteric domain. J. Biol. Chem. 269, 19777-19786.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19777-19786
    • Foster, B.A.1    Thomas, S.M.2    Mahr, J.A.3    Renosto, F.4    Patel, H.C.5    Segel, I.H.6
  • 23
    • 0028559230 scopus 로고
    • A P-loop motif in a widespread ATP pyrophosphatase domain: Implications for the evolution of sequence motifs and enzyme activity
    • Bork, P. and Koonin, E.V. (1994) A P-loop motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity. Protein Struct. Funct. Genet. 20, 347-355.
    • (1994) Protein Struct. Funct. Genet. , vol.20 , pp. 347-355
    • Bork, P.1    Koonin, E.V.2
  • 24
    • 0000122573 scopus 로고
    • PHYLIP-phylogeny inference package (version 3.2)
    • Felsenstein, J. (1989) PHYLIP-phylogeny inference package (version 3.2). Cladistics 5, 164-166.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 26
    • 0028055018 scopus 로고
    • The winds of (evolutionary) change: Breathing new life into microbiology
    • Olsen, J., Woese, C.R. and Overbeek, R. (1994) The winds of (evolutionary) change: breathing new life into microbiology. J. Bacteriol. 176, 1-6.
    • (1994) J. Bacteriol. , vol.176 , pp. 1-6
    • Olsen, J.1    Woese, C.R.2    Overbeek, R.3
  • 27
    • 0030821694 scopus 로고    scopus 로고
    • Towards the phylogeny of APS reductases and sirohaem sulfite reductases in sulfate-reducing and sulfur-oxidizing prokaryotes
    • Hipp, W.M., Pott, A.S., Thum-Schmitz, N., Faath, I., Dahl, C. and Trüper, H.G. (1997) Towards the phylogeny of APS reductases and sirohaem sulfite reductases in sulfate-reducing and sulfur-oxidizing prokaryotes. Microbiology 143, 2891-2902.
    • (1997) Microbiology , vol.143 , pp. 2891-2902
    • Hipp, W.M.1    Pott, A.S.2    Thum-Schmitz, N.3    Faath, I.4    Dahl, C.5    Trüper, H.G.6
  • 28
    • 0031913670 scopus 로고    scopus 로고
    • A dissimilatory sirohaem-sulfite reductase-type protein from the hyperthermophilic archaeon Pyrobaculum islandicum
    • Molitor, M., Dahl, C., Molitor, I., Schäfer, U., Speich, N., Huber, R., Deutzmann, R. and Trüper, H.G. (1998) A dissimilatory sirohaem-sulfite reductase-type protein from the hyperthermophilic archaeon Pyrobaculum islandicum. Microbiology 144, 529-541.
    • (1998) Microbiology , vol.144 , pp. 529-541
    • Molitor, M.1    Dahl, C.2    Molitor, I.3    Schäfer, U.4    Speich, N.5    Huber, R.6    Deutzmann, R.7    Trüper, H.G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.