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Volumn 26, Issue 5, 2004, Pages 437-442

Cloning, expression and characterization of glucose-1-phosphate thymidylyltransferase (strmlA) from Thermus caldophilus

Author keywords

dTDP L Rhamnose; Glucose 1 phosphate thymidylyltransferase; Hydrophobic and charged residues; Thermus caldophilus

Indexed keywords

GLUCOSE 1 PHOSPHATE THYMIDYLYLTRANSFERASE; GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE; NUCLEOTIDYLTRANSFERASE; RECOMBINANT PROTEIN;

EID: 1642279672     PISSN: 01415492     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:BILE.0000018264.35237.86     Document Type: Article
Times cited : (9)

References (20)
  • 1
    • 0034671801 scopus 로고    scopus 로고
    • The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA)
    • Blankenfeldt W, Asunction M, Lam JS, Naismith JH (2000) The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA). EMBO J. 19: 6652-6663.
    • (2000) EMBO J. , vol.19 , pp. 6652-6663
    • Blankenfeldt, W.1    Asunction, M.2    Lam, J.S.3    Naismith, J.H.4
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (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
  • 3
    • 0034677790 scopus 로고    scopus 로고
    • Elucidation of determinants of protein stability through genome sequence analysis
    • Chakravarty S, Varadarajan R (2000) Elucidation of determinants of protein stability through genome sequence analysis. FEBS Lett. 470: 65-69.
    • (2000) FEBS Lett. , vol.470 , pp. 65-69
    • Chakravarty, S.1    Varadarajan, R.2
  • 5
    • 0242290154 scopus 로고    scopus 로고
    • Thermophilic prokaryotes have characteristic patterns of codon usage, amino acid composition and nucleotide content
    • Gregory AC, Singer, Donal A, Hickey (2003) Thermophilic prokaryotes have characteristic patterns of codon usage, amino acid composition and nucleotide content. Gene 23: 39-47.
    • (2003) Gene , vol.23 , pp. 39-47
    • Gregory, A.C.1    Singer2    Donal, A.3    Hickey4
  • 6
    • 0032715527 scopus 로고    scopus 로고
    • Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteins
    • Gromiha MM, Oobatake M, Sarai A (1999) Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteins. Biophys. Chem. 82: 51-67.
    • (1999) Biophys. Chem. , vol.82 , pp. 51-67
    • Gromiha, M.M.1    Oobatake, M.2    Sarai, A.3
  • 7
    • 0030970741 scopus 로고    scopus 로고
    • Structural basis for thermostability and identification of potential active site residues for adenylate kinases from the archaeal genus Methanococcus
    • Haney P, Konisky J, Koretke KK, Luthey-Schulten Z, Wolynes PG (1997) Structural basis for thermostability and identification of potential active site residues for adenylate kinases from the archaeal genus Methanococcus. Protein Eng. 28: 117-130.
    • (1997) Protein Eng. , vol.28 , pp. 117-130
    • Haney, P.1    Konisky, J.2    Koretke, K.K.3    Luthey-Schulten, Z.4    Wolynes, P.G.5
  • 8
    • 0036097357 scopus 로고    scopus 로고
    • Cloning and expression of the gene for inorganic pyrophosphatase of Thermus caldophilus GK24 and properties of the enzyme
    • Kim YS, Lee DS, Kwon ST (2002) Cloning and expression of the gene for inorganic pyrophosphatase of Thermus caldophilus GK24 and properties of the enzyme. J. Microbiol. Biotechnol. 12: 301-305.
    • (2002) J. Microbiol. Biotechnol. , vol.12 , pp. 301-305
    • Kim, Y.S.1    Lee, D.S.2    Kwon, S.T.3
  • 9
    • 0038359368 scopus 로고    scopus 로고
    • Mechanistic study of the intramolecular conversion of maltose to trehalose by Thermus caldophilus GK24 trehalose synthase
    • Koh S, Kim J, Shin HJ, Lee DH, Bae J, Kim D, Lee DS (2003) Mechanistic study of the intramolecular conversion of maltose to trehalose by Thermus caldophilus GK24 trehalose synthase. Carbohyd. Res. 338: 1339-1343.
    • (2003) Carbohyd. Res. , vol.338 , pp. 1339-1343
    • Koh, S.1    Kim, J.2    Shin, H.J.3    Lee, D.H.4    Bae, J.5    Kim, D.6    Lee, D.S.7
  • 10
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein stability
    • Kumar S, Tsai CJ, Nussinov R (2000) Factors enhancing protein stability. Protein Eng. 13: 179-191.
    • (2000) Protein Eng. , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 11
    • 0028049079 scopus 로고
    • Purification, characterization and high performance liquid chromatography assay of salmonella glucose-1-phosphate cytidylyltransferase from the cloned rfbF gene
    • Lennart L, Kaiser R, Reeves PR, Lindberg AA (1994) Purification, characterization and high performance liquid chromatography assay of salmonella glucose-1-phosphate cytidylyltransferase from the cloned rfbF gene. J. Biol. Chem. 269: 122-126.
    • (1994) J. Biol. Chem. , vol.269 , pp. 122-126
    • Lennart, L.1    Kaiser, R.2    Reeves, P.R.3    Lindberg, A.A.4
  • 12
    • 0141814840 scopus 로고    scopus 로고
    • The variation of dTDP-L-rhamnose pathway genes in Vibrio cholerae
    • Li Q, Hobbs M, Reeves PR (2003) The variation of dTDP-L-rhamnose pathway genes in Vibrio cholerae. Microbiology 149: 2463-2474.
    • (2003) Microbiology , vol.149 , pp. 2463-2474
    • Li, Q.1    Hobbs, M.2    Reeves, P.R.3
  • 13
    • 0030950127 scopus 로고    scopus 로고
    • Determination of the pathway for rhamnose biosynthesis in mycobacteria: Cloning, sequencing and expression of the Mycobacterium tuberculosis gene encoding α-D-glucose-1-phosphate thymidylyltransferase
    • Ma Y, Mills JA, Belisle JT, Vissa V, Howell M, Bowlin K, Scherman MS, McNeil M (1997) Determination of the pathway for rhamnose biosynthesis in mycobacteria: cloning, sequencing and expression of the Mycobacterium tuberculosis gene encoding α-D-glucose-1-phosphate thymidylyltransferase. Microbiology 143: 937-945.
    • (1997) Microbiology , vol.143 , pp. 937-945
    • Ma, Y.1    Mills, J.A.2    Belisle, J.T.3    Vissa, V.4    Howell, M.5    Bowlin, K.6    Scherman, M.S.7    McNeil, M.8
  • 14
    • 0029560547 scopus 로고
    • Genetic analysis of the dTDP-rhamnose biosynthesis region of the Escherichia coli VW187 (O7:Kl) rfb gene cluster: Identification of functional homologs of rfbB and rfbA in the rff cluster and correct location of the rffE gene
    • Marolda CL, Valvano MA (1995) Genetic analysis of the dTDP-rhamnose biosynthesis region of the Escherichia coli VW187 (O7:Kl) rfb gene cluster: identification of functional homologs of rfbB and rfbA in the rff cluster and correct location of the rffE gene. J. Bacteriol. 177: 5539-5546.
    • (1995) J. Bacteriol. , vol.177 , pp. 5539-5546
    • Marolda, C.L.1    Valvano, M.A.2
  • 15
    • 0029932580 scopus 로고    scopus 로고
    • Analysis of protein conformational characteristics related to thermostability
    • Querol E, Perez-Pons JA, Mozo-Villarias A (1996) Analysis of protein conformational characteristics related to thermostability. Protein Eng. 9: 265-271.
    • (1996) Protein Eng. , vol.9 , pp. 265-271
    • Querol, E.1    Perez-Pons, J.A.2    Mozo-Villarias, A.3
  • 16
    • 0030741375 scopus 로고    scopus 로고
    • The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 A resolution
    • Russell RJ, Ferguson JM, Hough DW, Danson MJ, Taylor GL (1997) The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 A resolution. Biochemistry 36: 9983-9994.
    • (1997) Biochemistry , vol.36 , pp. 9983-9994
    • Russell, R.J.1    Ferguson, J.M.2    Hough, D.W.3    Danson, M.J.4    Taylor, G.L.5
  • 18
    • 0020122141 scopus 로고
    • Heat stable and fructose-1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium
    • Taguchi H, Yamashita H, Matsuzawa, Ohta T (1982) Heat stable and fructose-1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium. J. Biochem. 91: 1343-1348.
    • (1982) J. Biochem. , vol.91 , pp. 1343-1348
    • Taguchi, H.1    Yamashita, H.2    Matsuzawa3    Ohta, T.4
  • 19
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucl. Acids Res. 24: 4876-4882.
    • (1997) Nucl. Acids Res. , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 20
    • 0015437962 scopus 로고
    • Measurement of molecular weights by electrophoresis on SDS-polyacrylamide gel
    • Weber K, Pringle JR, Osborn M (1971) Measurement of molecular weights by electrophoresis on SDS-polyacrylamide gel. Meth. Enzymol. 26: 3-27.
    • (1971) Meth. Enzymol. , vol.26 , pp. 3-27
    • Weber, K.1    Pringle, J.R.2    Osborn, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.