메뉴 건너뛰기




Volumn 35, Issue 4, 2004, Pages 309-314

Mutagenesis of Escherichia coli uridine phosphorylase by random pentapeptide insertions

Author keywords

Escherichia coli; Mutagenesis; Transposon; Uridine phosphorylase

Indexed keywords

AMINO ACIDS; CATALYSIS; CRYSTAL STRUCTURE; ENZYMES; ESCHERICHIA COLI; PROTEINS;

EID: 3242875274     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2004.04.017     Document Type: Article
Times cited : (5)

References (24)
  • 1
    • 0017331267 scopus 로고
    • Uridine phosphorylase from Escherichia coli. Physical and chemical characterization
    • Leer J.C., Hammer J., Schwartz M. Uridine phosphorylase from Escherichia coli. Physical and chemical characterization. Eur. J. Biochem. 75:1977;217-224
    • (1977) Eur. J. Biochem. , vol.75 , pp. 217-224
    • Leer, J.C.1    Hammer, J.2    Schwartz, M.3
  • 2
    • 0022586525 scopus 로고
    • Uridine phosphorylase from Escherichia coli B. Enzymatic and molecular properties
    • Vita A., Amici A., Cacciamani T., Lanciotti M., Magni G. Uridine phosphorylase from Escherichia coli B. Enzymatic and molecular properties. Int. J. Biochem. 18:1986;431-435
    • (1986) Int. J. Biochem. , vol.18 , pp. 431-435
    • Vita, A.1    Amici, A.2    Cacciamani, T.3    Lanciotti, M.4    Magni, G.5
  • 3
    • 0036183496 scopus 로고    scopus 로고
    • Structural analyses reveal two distinct families of nucleoside phosphorylases
    • Pugmire M.J., Ealick S.E. Structural analyses reveal two distinct families of nucleoside phosphorylases. Biochem. J. 361:2002;1-25
    • (2002) Biochem. J. , vol.361 , pp. 1-25
    • Pugmire, M.J.1    Ealick, S.E.2
  • 4
    • 0038387947 scopus 로고    scopus 로고
    • Identification of a novel human uridine phosphorylase
    • Johansson M. Identification of a novel human uridine phosphorylase. Biochem. Biophys. Res. Commun. 307:2003;41-46
    • (2003) Biochem. Biophys. Res. Commun. , vol.307 , pp. 41-46
    • Johansson, M.1
  • 6
    • 0032479324 scopus 로고    scopus 로고
    • Crystal structure of the ternary complex of E. coli purine nucleoside phosphorylase with formycin B, a structural analogue of the substrate inosine, and phosphate (Sulphate) at 2.1 Å resolution
    • Koellner G., Luiç M., Shugar D., Saenger W., Bzowska A. Crystal structure of the ternary complex of E. coli purine nucleoside phosphorylase with formycin B, a structural analogue of the substrate inosine, and phosphate (Sulphate) at 2.1 Å resolution. J. Mol. Biol. 280:1998;153-166
    • (1998) J. Mol. Biol. , vol.280 , pp. 153-166
    • Koellner, G.1    Luiç, M.2    Shugar, D.3    Saenger, W.4    Bzowska, A.5
  • 7
    • 0036303728 scopus 로고    scopus 로고
    • Open and closed conformation of the E. coli purine nucleoside phosphorylase active center and implications for the catalytic mechanism
    • Koellner G., Bzowska A., Kutrowska Wielgus V., Luic M., Steiner P., Saenger W., et al. Open and closed conformation of the E. coli purine nucleoside phosphorylase active center and implications for the catalytic mechanism. J. Mol. Biol. 315:2002;351-371
    • (2002) J. Mol. Biol. , vol.315 , pp. 351-371
    • Koellner, G.1    Bzowska, A.2    Kutrowska Wielgus, V.3    Luic, M.4    Steiner, P.5    Saenger, W.6
  • 8
    • 0029716298 scopus 로고    scopus 로고
    • Protein engineering of uridine phosphorylase from Escherichia coli K-12. Study of the role of cysteine residues in enzyme function
    • Veiko V.P., Siprashvili Z.Z., Ratmanova K.I., Gul'ko L.V., Mironov A.A. Protein engineering of uridine phosphorylase from Escherichia coli K-12. Study of the role of cysteine residues in enzyme function. Mol. Biol. (Mosk). 30:1996;170-176
    • (1996) Mol. Biol. (Mosk) , vol.30 , pp. 170-176
    • Veiko, V.P.1    Siprashvili, Z.Z.2    Ratmanova, K.I.3    Gul'Ko, L.V.4    Mironov, A.A.5
  • 9
    • 0028967090 scopus 로고
    • Complete inactivation of Escherichia coli uridine phosphorylase by modification of Asp5 with Woodward's reagent K
    • Komissarov A.A., Romanova D.V., Debabov V.G. Complete inactivation of Escherichia coli uridine phosphorylase by modification of Asp5 with Woodward's reagent K. J. Biol. Chem. 270:1995;10050-10055
    • (1995) J. Biol. Chem. , vol.270 , pp. 10050-10055
    • Komissarov, A.A.1    Romanova, D.V.2    Debabov, V.G.3
  • 10
    • 0029396584 scopus 로고
    • Study of the role of histidine residues in the function of uridine phosphorylase from Escherichia coli K-12 by protein engineering
    • Veiko V.P., Siprashvili Z.Z., Ratmanova K.I., Gul K. Study of the role of histidine residues in the function of uridine phosphorylase from Escherichia coli K-12 by protein engineering. Bioorg. Khim. 21:1995;834-837
    • (1995) Bioorg. Khim. , vol.21 , pp. 834-837
    • Veiko, V.P.1    Siprashvili, Z.Z.2    Ratmanova, K.I.3    Gul, K.4
  • 11
    • 0025005569 scopus 로고
    • Modification of uridine phosphorylase from Escherichia coli by diethyl pyrocarbonate. Evidence for a histidine residue in the active site of the enzyme
    • Drabikowska A.K., Wozniak G. Modification of uridine phosphorylase from Escherichia coli by diethyl pyrocarbonate. Evidence for a histidine residue in the active site of the enzyme. Biochem. J. 270:1990;319-323
    • (1990) Biochem. J. , vol.270 , pp. 319-323
    • Drabikowska, A.K.1    Wozniak, G.2
  • 12
    • 0028879009 scopus 로고
    • Modification with tetranitromethane of an essential tyrosine residue in uridine phosphorylase from Escherichia coli
    • Komissarov A.A., Debabov V.G. Modification with tetranitromethane of an essential tyrosine residue in uridine phosphorylase from Escherichia coli. Biochim. Biophys. Acta. 1252:1995;239-244
    • (1995) Biochim. Biophys. Acta , vol.1252 , pp. 239-244
    • Komissarov, A.A.1    Debabov, V.G.2
  • 13
    • 3242890336 scopus 로고    scopus 로고
    • Immobilized biocatalysts for the production of nucleosides and nucleoside analogues by enzymatic transglycosylation reactions
    • in press.
    • Zuffi G, Ghisotti D, Oliva I, Capra E, Frascotti G, Tonon G, and Orsini, G. Immobilized biocatalysts for the production of nucleosides and nucleoside analogues by enzymatic transglycosylation reactions. Biocatal. Biotransformation, in press.
    • Biocatal. Biotransformation
    • Zuffi, G.1    Ghisotti, D.2    Oliva, I.3    Capra, E.4    Frascotti, G.5    Tonon, G.6    Orsini, G.7
  • 14
    • 0030825248 scopus 로고    scopus 로고
    • Pentapeptide scanning mutagenesis: Random insertion of a variable five amino acid cassette in a target protein
    • Hallet B., Sherratt D.J., Hayes F. Pentapeptide scanning mutagenesis: random insertion of a variable five amino acid cassette in a target protein. Nucleic Acids Res. 25:1997;1866-1867
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1866-1867
    • Hallet, B.1    Sherratt, D.J.2    Hayes, F.3
  • 15
    • 0028957964 scopus 로고
    • Control of transcription termination by an RNA factor in bacteriophage P4 immunity: Identification of the target sites
    • Sabbattini P., Forti F., Ghisotti D., Dehò G. Control of transcription termination by an RNA factor in bacteriophage P4 immunity: identification of the target sites. J. Bacteriol. 177:1995;1425-1434
    • (1995) J. Bacteriol. , vol.177 , pp. 1425-1434
    • Sabbattini, P.1    Forti, F.2    Ghisotti, D.3    Dehò, G.4
  • 16
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:1983;557-580
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 17
    • 0023968566 scopus 로고
    • Resolution of ColE1 dimers requires a DNA sequence implicated in the three-dimensional organization of the cer site
    • Summers D.K., Sherratt D.J. Resolution of ColE1 dimers requires a DNA sequence implicated in the three-dimensional organization of the cer site. EMBO J. 7:1988;851-858
    • (1988) EMBO J. , vol.7 , pp. 851-858
    • Summers, D.K.1    Sherratt, D.J.2
  • 18
    • 0024008186 scopus 로고
    • Structural and functional analysis of Tn4430: Identification of an integrase-like protein involved in the co-integrate-resolution process
    • Mahillon J., Lereclus D. Structural and functional analysis of Tn4430: identification of an integrase-like protein involved in the co-integrate- resolution process. EMBO J. 7:1988;1515-1526
    • (1988) EMBO J. , vol.7 , pp. 1515-1526
    • Mahillon, J.1    Lereclus, D.2
  • 19
    • 0020442864 scopus 로고
    • The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
    • Vieira J., Messing J. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene. 19:1982;259-268
    • (1982) Gene , vol.19 , pp. 259-268
    • Vieira, J.1    Messing, J.2
  • 20
    • 0028227829 scopus 로고
    • Cloning vectors for the synthesis of epitope-tagged, truncated and chimeric proteins in Saccharomyces cerevisiae
    • Foreman P.K., Davis R.W. Cloning vectors for the synthesis of epitope-tagged, truncated and chimeric proteins in Saccharomyces cerevisiae. Gene. 144:1994;63-68
    • (1994) Gene , vol.144 , pp. 63-68
    • Foreman, P.K.1    Davis, R.W.2
  • 21
    • 0034548711 scopus 로고    scopus 로고
    • Pentapeptide scanning mutagenesis: Encouraging old proteins to execute unusual tricks
    • Hayes F., Hallet B. Pentapeptide scanning mutagenesis: encouraging old proteins to execute unusual tricks. Trends Microbiol. 8:2000;571-577
    • (2000) Trends Microbiol. , vol.8 , pp. 571-577
    • Hayes, F.1    Hallet, B.2
  • 22
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 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., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 24
    • 0027198862 scopus 로고
    • Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases
    • Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C., Watanabe C. Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc. Natl. Acad. Sci. USA. 90:1993;5011-5015
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5011-5015
    • Henzel, W.J.1    Billeci, T.M.2    Stults, J.T.3    Wong, S.C.4    Grimley, C.5    Watanabe, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.