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Volumn 65, Issue 5, 2001, Pages 1230-1235

gsk Disruption Leads to Guanosine Accumulation in Escherichia coli

Author keywords

Escherichia coli; gsk; guaB; guaC gene; Guanosine production; Inosine

Indexed keywords

GUANOSINE; INOSINE KINASE; PHOSPHOTRANSFERASE;

EID: 0035346490     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.65.1230     Document Type: Article
Times cited : (7)

References (23)
  • 1
    • 0041457883 scopus 로고
    • Studies on the fermentative production of purine derivatives. Part I. Derivation of guanosine and inosine-producing mutants from a Bacillus strain
    • Nogami, I., Kida, M., Iijima, T., and Yoneda, M., Studies on the fermentative production of purine derivatives. Part I. Derivation of guanosine and inosine-producing mutants from a Bacillus strain. Agric. Biol. Chem., 32, 144-152 (1968).
    • (1968) Agric. Biol. Chem. , vol.32 , pp. 144-152
    • Nogami, I.1    Kida, M.2    Iijima, T.3    Yoneda, M.4
  • 2
    • 0013627959 scopus 로고
    • Improved inosine production and derepression of purine nucleotide biosynthetic enzymes in 8-azaguanine resistant mutants of Bacillus subtilis
    • Ishii, K. and Shiio, I., Improved inosine production and derepression of purine nucleotide biosynthetic enzymes in 8-azaguanine resistant mutants of Bacillus subtilis. Agric. Biol. Chem., 36, 1511-1522 (1972).
    • (1972) Agric. Biol. Chem. , vol.36 , pp. 1511-1522
    • Ishii, K.1    Shiio, I.2
  • 3
    • 0000452467 scopus 로고
    • 5′-Nucleotidase activity in improved inosine-producing mutants of Bacillus subtilis
    • Matsui, H., Sato, K., Enei, H., and Takinami, K., 5′-Nucleotidase activity in improved inosine-producing mutants of Bacillus subtilis. Agric. Biol. Chem., 46, 2347-2352 (1982).
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 2347-2352
    • Matsui, H.1    Sato, K.2    Enei, H.3    Takinami, K.4
  • 4
    • 0018589037 scopus 로고
    • Production of guanosine by psicofuranine and decoyinine resistant mutants of Bacillus subtilis
    • Matsui, H., Sato, K., Enei, H., and Hirose, Y., Production of guanosine by psicofuranine and decoyinine resistant mutants of Bacillus subtilis. Agric. Biol. Chem., 43, 1739-1744 (1979).
    • (1979) Agric. Biol. Chem. , vol.43 , pp. 1739-1744
    • Matsui, H.1    Sato, K.2    Enei, H.3    Hirose, Y.4
  • 5
    • 0014829178 scopus 로고
    • Production of nucleic acid-related substances by fermentation processes. XXXIII. Accumulation of inosine by a mutant of Brevibacterium ammoniagenes
    • Furuya, A., Abe, S., and Kinoshita, S., Production of nucleic acid-related substances by fermentation processes. XXXIII. Accumulation of inosine by a mutant of Brevibacterium ammoniagenes. Appl. Microbiol., 20, 263-270 (1970).
    • (1970) Appl. Microbiol. , vol.20 , pp. 263-270
    • Furuya, A.1    Abe, S.2    Kinoshita, S.3
  • 6
    • 0017812424 scopus 로고
    • Inosine accumulation by mutants of Brevibacterium ammoniagenes strain improvement and culture conditions
    • Kotani, Y., Yamaguchi, K., Kato, F., and Furuya, A., Inosine accumulation by mutants of Brevibacterium ammoniagenes strain improvement and culture conditions. Agric. Biol. Chem., 42, 399-405 (1978).
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 399-405
    • Kotani, Y.1    Yamaguchi, K.2    Kato, F.3    Furuya, A.4
  • 8
    • 0035293796 scopus 로고    scopus 로고
    • Investigation of various genotype characteristics for inosine accumulation in Escherichia coli W3110
    • Matsui, H., Kawasaki, H., Shimaoka, M., and Kurahashi, O., Investigation of various genotype characteristics for inosine accumulation in Escherichia coli W3110. Biosci. Biotechnol. Biochem., 65, 570-578 (2001).
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 570-578
    • Matsui, H.1    Kawasaki, H.2    Shimaoka, M.3    Kurahashi, O.4
  • 9
    • 0020478925 scopus 로고
    • Nucleotide sequence of Escherichia coli purF and deduced amino acid sequence of glutamine phosphoribosylpyrophosphate amido-transferase
    • Tso, J. Y., Zalkin, H., van Cleemput, M., Yanofsky, C., and Smith, J. M., Nucleotide sequence of Escherichia coli purF and deduced amino acid sequence of glutamine phosphoribosylpyrophosphate amido-transferase. J. Biol. Chem., 257, 3525-3531 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 3525-3531
    • Tso, J.Y.1    Zalkin, H.2    Van Cleemput, M.3    Yanofsky, C.4    Smith, J.M.5
  • 10
    • 0024242338 scopus 로고
    • Nucleotide sequence and analysis of the purA gene encoding adenylosuccinate synthetase of Escherichia coli K12
    • Wolfe, S. A. and Smith, J. M., Nucleotide sequence and analysis of the purA gene encoding adenylosuccinate synthetase of Escherichia coli K12. J. Biol. Chem., 263, 19147-19153 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 19147-19153
    • Wolfe, S.A.1    Smith, J.M.2
  • 11
    • 0025784230 scopus 로고
    • Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol
    • Hershfield, M. S., Chaffee, S., Koro-Johnson, L., Mary, A., Smith, A. A., and Sort, S. A., Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol. Proc. Natl. Acad. Sci. U.S.A., 88, 7185-7189 (1991).
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 7185-7189
    • Hershfield, M.S.1    Chaffee, S.2    Koro-Johnson, L.3    Mary, A.4    Smith, A.A.5    Sort, S.A.6
  • 12
    • 0024263352 scopus 로고
    • Escherichia coli gene purR encoding a repressor protein for purine nucleotides synthesis
    • Rolfes, R. J. and Zalkin, H., Escherichia coli gene purR encoding a repressor protein for purine nucleotides synthesis. J. Biol. Chem., 263, 19653-19661 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 19653-19661
    • Rolfes, R.J.1    Zalkin, H.2
  • 13
    • 0026018939 scopus 로고
    • Deduced amino acid sequence of Escherichia coli adenosine deaminase reveals evolutionarily conserved amino acid residues:Implications for catalytic function
    • Chang, Z., Nygaard, P., Chinault, A. C., and Kellems, R. E., Deduced amino acid sequence of Escherichia coli adenosine deaminase reveals evolutionarily conserved amino acid residues:Implications for catalytic function. Biochemistry, 30, 2273-2280 (1991).
    • (1991) Biochemistry , vol.30 , pp. 2273-2280
    • Chang, Z.1    Nygaard, P.2    Chinault, A.C.3    Kellems, R.E.4
  • 14
    • 0028355801 scopus 로고
    • Binding of purine nucleotides to two regulatory sites results in synergistic feedback inhibition of glutamine 5-phosphoribosylpyrophosphate amidotransferase
    • Zhou, G., Smith, J. L., and Zalkin, H., Binding of purine nucleotides to two regulatory sites results in synergistic feedback inhibition of glutamine 5-phosphoribosylpyrophosphate amidotransferase. J. Biol. Chem., 269, 6784-6789 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 6784-6789
    • Zhou, G.1    Smith, J.L.2    Zalkin, H.3
  • 15
    • 0022431880 scopus 로고
    • Nucleotide sequence of the guaB locus encoding IMP dehydrogenase of Escherichia coli K12
    • Tiedeman, A. A. and Smith, J. M., Nucleotide sequence of the guaB locus encoding IMP dehydrogenase of Escherichia coli K12. Nucleic Acids Res., 13, 1303-1316 (1985).
    • (1985) Nucleic Acids Res. , vol.13 , pp. 1303-1316
    • Tiedeman, A.A.1    Smith, J.M.2
  • 16
    • 0029093265 scopus 로고
    • Cloning of a guanosine-inosine kinase gene of Escherichia coli and characterization of the purified gene product
    • Mori, H., Iida, A., Teshiba, S., and Fujio, T., Cloning of a guanosine-inosine kinase gene of Escherichia coli and characterization of the purified gene product. J. Bacteriol., 177, 4921-4926 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 4921-4926
    • Mori, H.1    Iida, A.2    Teshiba, S.3    Fujio, T.4
  • 17
    • 0015451273 scopus 로고
    • Pedigrees of some mutant strains of Escherichia coli K-12
    • Bachmann, B. J., Pedigrees of some mutant strains of Escherichia coli K-12. Bacteriol. Rev., 36, 525-530 (1972).
    • (1972) Bacteriol. Rev. , vol.36 , pp. 525-530
    • Bachmann, B.J.1
  • 19
    • 0021802990 scopus 로고
    • Construction and characterization of a deletion mutant lacking micF, a proposed regulatory gene for OmpF synthesis in Escherichia coli
    • Matsuyama, S. and Mizushima, S., Construction and characterization of a deletion mutant lacking micF, a proposed regulatory gene for OmpF synthesis in Escherichia coli. J. Bacteriol., 162, 1196-1202 (1985).
    • (1985) J. Bacteriol. , vol.162 , pp. 1196-1202
    • Matsuyama, S.1    Mizushima, S.2
  • 20
    • 0018600265 scopus 로고
    • Inosine 5′-monophosphate dehydrogenase of Escherichia coli: Purification by affinity chromatography, subunit structure and inhibition by guanosine 5′-monophosphate
    • Gilbert, H. J., Lowe, C. R., and Drabble, W. T., Inosine 5′-monophosphate dehydrogenase of Escherichia coli: purification by affinity chromatography, subunit structure and inhibition by guanosine 5′-monophosphate. Biochem. J., 183, 481-494 (1979).
    • (1979) Biochem. J. , vol.183 , pp. 481-494
    • Gilbert, H.J.1    Lowe, C.R.2    Drabble, W.T.3
  • 21
    • 0023711405 scopus 로고
    • Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12
    • Andrews, S. C. and Guest, J. R., Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12. Biochem. J., 255, 35-43 (1988).
    • (1988) Biochem. J. , vol.255 , pp. 35-43
    • Andrews, S.C.1    Guest, J.R.2
  • 22
    • 0033605268 scopus 로고    scopus 로고
    • Inhibition of cellular growth by increased guanine nucleotide pools
    • Petersen, C., Inhibition of cellular growth by increased guanine nucleotide pools. J. Biol. Chem., 274, 5348-5356 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 5348-5356
    • Petersen, C.1
  • 23
    • 0024361644 scopus 로고
    • Characterization of the Escherichia coli prsA1-encoded mutant phosphoribosylpyrophosphate synthetase identifies a divalent cation-nucleotide binding site
    • Bower, S. G., Harlow, K. W., Switzer, R. L., and Hove-Jansen, B., Characterization of the Escherichia coli prsA1-encoded mutant phosphoribosylpyrophosphate synthetase identifies a divalent cation-nucleotide binding site. J. Biol. Chem., 264, 10287-10291 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 10287-10291
    • Bower, S.G.1    Harlow, K.W.2    Switzer, R.L.3    Hove-Jansen, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.