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Volumn 182, Issue 4, 2000, Pages 869-873

Genetic and biochemical characterization of Salmonella enterica serovar typhi deoxyribokinase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; PHOSPHOTRANSFERASE;

EID: 0033956360     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.4.869-873.2000     Document Type: Article
Times cited : (10)

References (23)
  • 2
    • 0025778670 scopus 로고
    • Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives
    • Bartolomé, B., J. Jubite, E. Martinez, and F. de la Cruz. 1991. Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives. Gene 102:75-78.
    • (1991) Gene , vol.102 , pp. 75-78
    • Bartolomé, B.1    Jubite, J.2    Martinez, E.3    De La Cruz, F.4
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0014291744 scopus 로고
    • Inability of low thymine-requiring mutants of Escherichia coli lacking phosphodeoxyribomutase to be induced for deoxythymidine phosphorylase and deoxyriboaldolase
    • Breitman, T. R., and R. M. Bradford. 1968. Inability of low thymine-requiring mutants of Escherichia coli lacking phosphodeoxyribomutase to be induced for deoxythymidine phosphorylase and deoxyriboaldolase. J. Bacteriol. 95:2434-2435.
    • (1968) J. Bacteriol. , vol.95 , pp. 2434-2435
    • Breitman, T.R.1    Bradford, R.M.2
  • 6
    • 0141955611 scopus 로고
    • Pentose fermentation by Lactobacillus plantarum. V. Fermentation of 2-deoxy-D-ribose
    • Domagk, G. G., and B. L. Horecker. 1958. Pentose fermentation by Lactobacillus plantarum. V. Fermentation of 2-deoxy-D-ribose. J. Biol. Chem. 233: 283-286.
    • (1958) J. Biol. Chem. , vol.233 , pp. 283-286
    • Domagk, G.G.1    Horecker, B.L.2
  • 7
    • 20644445532 scopus 로고
    • A deoxyribokinase from Lactobacillus plantarum
    • Ginsburg, A. 1958. A deoxyribokinase from Lactobacillus plantarum. J. Biol. Chem. 234:481-487.
    • (1958) J. Biol. Chem. , vol.234 , pp. 481-487
    • Ginsburg, A.1
  • 8
    • 0014250428 scopus 로고
    • 2-Deoxyribose gene-enzyme complex in Salmonella typhimurium. I. Isolation and enzymatic characterization of 2-deoxyribose-negative mutants
    • Hoffee, P. A. 1968. 2-Deoxyribose gene-enzyme complex in Salmonella typhimurium. I. Isolation and enzymatic characterization of 2-deoxyribose-negative mutants. J. Bacteriol. 95:449-457.
    • (1968) J. Bacteriol. , vol.95 , pp. 449-457
    • Hoffee, P.A.1
  • 9
    • 0026643236 scopus 로고
    • Structure and function of the uhp genes for the sugar phosphate transport system in Escherichia coli and Salmonella typhimurium
    • Island, M. D., B. Y. Wei, and R. J. Kadner. 1992. Structure and function of the uhp genes for the sugar phosphate transport system in Escherichia coli and Salmonella typhimurium. J. Bacteriol. 174:2754-2762.
    • (1992) J. Bacteriol. , vol.174 , pp. 2754-2762
    • Island, M.D.1    Wei, B.Y.2    Kadner, R.J.3
  • 10
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., J. Y. Zou, S. W. Cowan, and M. Kjeildgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47:110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeildgaard, M.4
  • 11
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0026027810 scopus 로고
    • Isolation and characterization of catalytic and calmodulin-binding domains of Bordetella pertussis adenylate cyclase
    • Munier, H., A.-M. Gilles, P. Glaser, E. Krin, A. Danchin, R. S. Sarfati, and O. Bârzu. 1991. Isolation and characterization of catalytic and calmodulin-binding domains of Bordetella pertussis adenylate cyclase. Eur. J. Biochem. 196:469-474.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 469-474
    • Munier, H.1    Gilles, A.-M.2    Glaser, P.3    Krin, E.4    Danchin, A.5    Sarfati, R.S.6    Bârzu, O.7
  • 15
    • 0027772882 scopus 로고
    • Directed evolution of biosynthetic pathways. Recruitment of cysteine thioethers for constructing the cell wall of Escherichia coli
    • Richaud, C., D. Mengin-Lecreulx, S. Pochet, E. J. Johnson, G. N. Cohen, and P. Marlière. 1993. Directed evolution of biosynthetic pathways. Recruitment of cysteine thioethers for constructing the cell wall of Escherichia coli. J. Biol. Chem. 268:26827-26835.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26827-26835
    • Richaud, C.1    Mengin-Lecreulx, D.2    Pochet, S.3    Johnson, E.J.4    Cohen, G.N.5    Marlière, P.6
  • 16
    • 0014807638 scopus 로고
    • Genetic regulation of ribonucleoside and deoxyribonucleoside catabolism in Salmonella typhimurium
    • Robertson, B. C., P. Jargiello, J. Blank, and P. A. Hoffee. 1970. Genetic regulation of ribonucleoside and deoxyribonucleoside catabolism in Salmonella typhimurium. J. Bacteriol. 102:628-635.
    • (1970) J. Bacteriol. , vol.102 , pp. 628-635
    • Robertson, B.C.1    Jargiello, P.2    Blank, J.3    Hoffee, P.A.4
  • 20
    • 0030700505 scopus 로고    scopus 로고
    • Purification, characterization, and crystallization of Escherichia coli ribokinase
    • Sigrell, J. A., A. D. Cameron, T. A. Jones, and S. L. Mowbray. 1997. Purification, characterization, and crystallization of Escherichia coli ribokinase. Protein Sci. 6:2474-2476.
    • (1997) Protein Sci. , vol.6 , pp. 2474-2476
    • Sigrell, J.A.1    Cameron, A.D.2    Jones, T.A.3    Mowbray, S.L.4
  • 21
    • 0032520213 scopus 로고    scopus 로고
    • Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 Å resolution: Insights into a new family of kinase structures
    • Sigrell, J. A., A. D. Cameron, T. A. Jones, and S. L. Mowbray. 1998. Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 Å resolution: insights into a new family of kinase structures. Structure 6:183-193.
    • (1998) Structure , vol.6 , pp. 183-193
    • Sigrell, J.A.1    Cameron, A.D.2    Jones, T.A.3    Mowbray, S.L.4
  • 23
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.