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Volumn 174, Issue 2, 1999, Pages 239-246

The molybdenum cofactor biosynthesis protein MobA from Rhodobacter capsulatus is required for the activity of molybdenum enzymes containing MGD, but not for xanthine dehydrogenase harboring the MPT cofactor

Author keywords

HMP, hypoxanthine monophosphate; MGD, molybdopterin guanine dinucleotide; mob locus; Molybdenum cofactor biosynthesis; Molybdoenzyme; Molybdopterin guanine dinucleotide synthase; MPT, molybdopterin; Rhodobacter capsulatus

Indexed keywords

DIMETHYL SULFOXIDE; MOLYBDENUM; MOLYBDENUM ENZYME; MOLYBDOPTERIN GUANINE DINUCLEOTIDE SYNTHASE; NITRATE REDUCTASE; OXIDOREDUCTASE; UNCLASSIFIED DRUG; XANTHINE DEHYDROGENASE;

EID: 16744365314     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(99)00147-0     Document Type: Article
Times cited : (17)

References (28)
  • 1
    • 15444350252 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli K-12
    • Blattner, F.R. et al. (1997) The complete genome sequence of Escherichia coli K-12. Science 277, 1453-1462.
    • (1997) Science , vol.277 , pp. 1453-1462
    • Blattner, F.R.1
  • 2
    • 0025866022 scopus 로고
    • Molybdopterin adenine dinucleotide and molybdopterin hypoxanthine dinucleotide in formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum (Marburg)
    • Börner, G., Karrasch, M. and Thauer, R.K. (1991) Molybdopterin adenine dinucleotide and molybdopterin hypoxanthine dinucleotide in formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum (Marburg). FEBS Lett. 290, 31-34.
    • (1991) FEBS Lett. , vol.290 , pp. 31-34
    • Börner, G.1    Karrasch, M.2    Thauer, R.K.3
  • 3
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii
    • Bull, C.J. et al. (1996) Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273, 1058-1073.
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bull, C.J.1
  • 4
    • 0025105632 scopus 로고
    • An Fnr-like protein encoded in Rhizobium leguminosarum biovar viciae shows structural and functional homology to Rhizobium meliloti FixK
    • Colonna-Romano, S., Arnold, W., Schlüter, A., Boistard, P., Pühler, A. and Priefer, U.B. (1990) An Fnr-like protein encoded in Rhizobium leguminosarum biovar viciae shows structural and functional homology to Rhizobium meliloti FixK. Mol. Gen. Genet. 223, 138-147.
    • (1990) Mol. Gen. Genet. , vol.223 , pp. 138-147
    • Colonna-Romano, S.1    Arnold, W.2    Schlüter, A.3    Boistard, P.4    Pühler, A.5    Priefer, U.B.6
  • 5
    • 0031005344 scopus 로고    scopus 로고
    • The product of the molybdenum cofactor gene mobB of Escherichia coli is a GTP-binding protein
    • Eaves, D.J., Palmer, T. and Boxer, D.H. (1997) The product of the molybdenum cofactor gene mobB of Escherichia coli is a GTP-binding protein. Eur. J. Biochem. 246, 690-697.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 690-697
    • Eaves, D.J.1    Palmer, T.2    Boxer, D.H.3
  • 6
    • 0029653518 scopus 로고
    • Whole-genome random sequencing and assembly of Haemophilus influenzae Rd
    • Fleischmann, R.D. et al. (1995) Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269, 496-512.
    • (1995) Science , vol.269 , pp. 496-512
    • Fleischmann, R.D.1
  • 7
    • 0014670082 scopus 로고
    • Further purification and properties of Neurospora nitrate reductase
    • Garrett, R.H. and Nason, A. (1969) Further purification and properties of Neurospora nitrate reductase. J. Biol. Chem. 244, 2870-2882.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2870-2882
    • Garrett, R.H.1    Nason, A.2
  • 8
    • 0015274902 scopus 로고
    • Comparison of nitrate reductase mutants of Escherichia coli selected by alternative procedures
    • Glaser, J.H. and DeMoss, J.A. (1972) Comparison of nitrate reductase mutants of Escherichia coli selected by alternative procedures. Mol. Gen. Genet. 116, 1-10.
    • (1972) Mol. Gen. Genet. , vol.116 , pp. 1-10
    • Glaser, J.H.1    Demoss, J.A.2
  • 9
    • 0029101827 scopus 로고
    • The mob locus of Escherichia coli K12 required for molybdenum cofactor biosynthesis is expressed at very low levels
    • Iobbi-Nivol, C., Palmer, T., Whitty, P.W., McNairn, E. and Boxer, D.H. (1995) The mob locus of Escherichia coli K12 required for molybdenum cofactor biosynthesis is expressed at very low levels. Microbiology 141, 1663-1671.
    • (1995) Microbiology , vol.141 , pp. 1663-1671
    • Iobbi-Nivol, C.1    Palmer, T.2    Whitty, P.W.3    McNairn, E.4    Boxer, D.H.5
  • 10
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC 6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko, T. et al. (1996) Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC 6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 3, 109-136.
    • (1996) DNA Res. , vol.3 , pp. 109-136
    • Kaneko, T.1
  • 11
    • 0023957575 scopus 로고
    • Identification and mapping of nitrogen fixation genes of Rhodobacter capsulatus: Duplication of a nifA-nifB region
    • Klipp, W., Masepohl, B. and Pühler, A. (1988) Identification and mapping of nitrogen fixation genes of Rhodobacter capsulatus: duplication of a nifA-nifB region. J. Bacteriol. 170, 693-699.
    • (1988) J. Bacteriol. , vol.170 , pp. 693-699
    • Klipp, W.1    Masepohl, B.2    Pühler, A.3
  • 12
    • 0025368819 scopus 로고
    • A new family of RSF1010-derived expression and lac-fusion broad-host-range vectors for Gram-negative bacteria
    • Labes, M., Pühler, A. and Simon, R. (1990) A new family of RSF1010-derived expression and lac-fusion broad-host-range vectors for Gram-negative bacteria. Gene 89, 37-46.
    • (1990) Gene , vol.89 , pp. 37-46
    • Labes, M.1    Pühler, A.2    Simon, R.3
  • 13
    • 0031940235 scopus 로고    scopus 로고
    • Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulatus is more similar to its eukaryotic counterparts than to prokaryotic molybdenum enzymes
    • Leimkühler, S., Kern, M., Solomon, P.S., McEwan, A.G., Schwarz, G., Mendel, R.R. and Klipp, W. (1998) Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulatus is more similar to its eukaryotic counterparts than to prokaryotic molybdenum enzymes. Mol. Microbiol. 27, 853-869.
    • (1998) Mol. Microbiol. , vol.27 , pp. 853-869
    • Leimkühler, S.1    Kern, M.2    Solomon, P.S.3    McEwan, A.G.4    Schwarz, G.5    Mendel, R.R.6    Klipp, W.7
  • 14
    • 0021913760 scopus 로고
    • Periplasmic location of the terminal reductase in trimethylamine N-oxide and dimethylsulfoxide respiration in the photosynthetic bacterium Rhodopseudomonas capsulata
    • McEwan, A.G., Wetzstein, H.G., Ferguson, S.J. and Jackson, J.B. (1985) Periplasmic location of the terminal reductase in trimethylamine N-oxide and dimethylsulfoxide respiration in the photosynthetic bacterium Rhodopseudomonas capsulata. Biochim. Biophys. Acta 806, 410-417.
    • (1985) Biochim. Biophys. Acta , vol.806 , pp. 410-417
    • McEwan, A.G.1    Wetzstein, H.G.2    Ferguson, S.J.3    Jackson, J.B.4
  • 16
    • 0028338273 scopus 로고
    • Isolation of protein FA, a product of the mob locus required for molybdenum cofactor biosynthesis in Escherichia coli
    • Palmer, T., Vasishta, A., Whitty, P.W. and Boxer, D.H. (1994) Isolation of protein FA, a product of the mob locus required for molybdenum cofactor biosynthesis in Escherichia coli. Eur. J. Biochem. 222, 687-692.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 687-692
    • Palmer, T.1    Vasishta, A.2    Whitty, P.W.3    Boxer, D.H.4
  • 17
    • 0029882611 scopus 로고    scopus 로고
    • Involvement of the narJ and mob gene products in distinct steps in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli
    • Palmer, T., Santini, C.-L., Iobbi-Nivol, C., Eaves, D.J., Boxer, D.H. and Giordano, G. (1996) Involvement of the narJ and mob gene products in distinct steps in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli. Mol. Microbiol. 20, 875-884.
    • (1996) Mol. Microbiol. , vol.20 , pp. 875-884
    • Palmer, T.1    Santini, C.-L.2    Iobbi-Nivol, C.3    Eaves, D.J.4    Boxer, D.H.5    Giordano, G.6
  • 18
    • 0032554073 scopus 로고    scopus 로고
    • Characterization of the mob locus from Rhodobacter sphaeroides required for molybdenum cofactor biosynthesis
    • Palmer, T., Goodfellow, I.P.G., Sockett, R.E., McEwan, A.G. and Boxer, D.H. (1998) Characterization of the mob locus from Rhodobacter sphaeroides required for molybdenum cofactor biosynthesis. Biochim. Biophys. Acta 1395, 135-140.
    • (1998) Biochim. Biophys. Acta , vol.1395 , pp. 135-140
    • Palmer, T.1    Goodfellow, I.P.G.2    Sockett, R.E.3    McEwan, A.G.4    Boxer, D.H.5
  • 19
    • 0026669725 scopus 로고
    • The pterin molybdenum cofactors
    • Rajagopalan, K.V. and Johnson, J.L. (1992) The pterin molybdenum cofactors. J. Biol. Chem. 267, 10199-10202.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10199-10202
    • Rajagopalan, K.V.1    Johnson, J.L.2
  • 20
    • 0029881191 scopus 로고    scopus 로고
    • Isolation of periplasmic nitrate reductase genes from Rhodobacter sphaeroides DSM 158: Structural and functional differences among prokaryotic nitrate reductases
    • Reyes, F., Roldan, M.D., Klipp, W., Castillo, F. and Moreno-Vivian, C. (1996) Isolation of periplasmic nitrate reductase genes from Rhodobacter sphaeroides DSM 158: structural and functional differences among prokaryotic nitrate reductases. Mol. Microbiol. 19, 1307-1318.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1307-1318
    • Reyes, F.1    Roldan, M.D.2    Klipp, W.3    Castillo, F.4    Moreno-Vivian, C.5
  • 21
    • 0027298448 scopus 로고
    • Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis
    • Rivers, S.L., McNairn, E., Blasco, F., Giordano, G. and Boxer, D.H. (1993) Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis. Mol. Microbiol. 8, 1071-1081.
    • (1993) Mol. Microbiol. , vol.8 , pp. 1071-1081
    • Rivers, S.L.1    McNairn, E.2    Blasco, F.3    Giordano, G.4    Boxer, D.H.5
  • 23
    • 0030592449 scopus 로고    scopus 로고
    • Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 Å resolution
    • Schneider, F., Löwe, J., Huber, R., Schindelin, H., Kisker, C. and Knäblein, J. (1996) Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 Å resolution. J. Mol. Biol. 263, 53-69.
    • (1996) J. Mol. Biol. , vol.263 , pp. 53-69
    • Schneider, F.1    Löwe, J.2    Huber, R.3    Schindelin, H.4    Kisker, C.5    Knäblein, J.6
  • 24
    • 0000655643 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the dimethylsulfoxide reductase structural gene from Rhodobacter capsulatus
    • Shaw, A.L., Hanson, G.R. and McEwan, A.G. (1996) Cloning and sequence analysis of the dimethylsulfoxide reductase structural gene from Rhodobacter capsulatus. Biochim. Biophys. Acta 1276, 176-180.
    • (1996) Biochim. Biophys. Acta , vol.1276 , pp. 176-180
    • Shaw, A.L.1    Hanson, G.R.2    McEwan, A.G.3
  • 25
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram-negative bacteria
    • Simon, R., Priefer, U. and Pühler, A. (1983) A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram-negative bacteria. BioTechnology 1, 784-791.
    • (1983) BioTechnology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 27
    • 0020442864 scopus 로고
    • The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
    • Vieira, J. and Messing, J. (1982) The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19, 259-268.
    • (1982) Gene , vol.19 , pp. 259-268
    • Vieira, J.1    Messing, J.2
  • 28
    • 0027175827 scopus 로고
    • Characterization of Rhodobacter capsulatus genes encoding a molybdenum transport system and putative molybdenum-pterin-binding proteins
    • Wang, G., Angermüller, S. and Klipp, W. (1993) Characterization of Rhodobacter capsulatus genes encoding a molybdenum transport system and putative molybdenum-pterin-binding proteins. J. Bacteriol. 175, 3031-3042.
    • (1993) J. Bacteriol. , vol.175 , pp. 3031-3042
    • Wang, G.1    Angermüller, S.2    Klipp, W.3


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