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Volumn 373, Issue 1, 2008, Pages 8-13

Active site of mycobacterial dUTPase: Structural characteristics and a built-in sensor

Author keywords

dUTPase; Enzyme kinetics; Fluorescence spectroscopy; Inhibitor screening; Mycobacterium tuberculosis; Pyrophosphate assay; Tryptophan sensor; Tuberculosis; Uracil

Indexed keywords

ALPHA,BETA IMIDO DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; BACTERIAL ENZYME; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; HISTIDINE; MAGNESIUM ION; TETRAPEPTIDE; TRYPTOPHAN;

EID: 45849136329     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.05.130     Document Type: Article
Times cited : (60)

References (25)
  • 2
    • 34248181891 scopus 로고    scopus 로고
    • Barriers to reaching the targets for tuberculosis control: multidrug-resistant tuberculosis
    • discussion 391-384
    • Blondal K. Barriers to reaching the targets for tuberculosis control: multidrug-resistant tuberculosis. Bull. World Health Organ. 85 (2007) 387-390 discussion 391-384
    • (2007) Bull. World Health Organ. , vol.85 , pp. 387-390
    • Blondal, K.1
  • 3
    • 34248636300 scopus 로고    scopus 로고
    • Current strategies for identifying and validating targets for new treatment-shortening drugs for TB
    • Williams K.J., and Duncan K. Current strategies for identifying and validating targets for new treatment-shortening drugs for TB. Curr. Mol. Med. 7 (2007) 297-307
    • (2007) Curr. Mol. Med. , vol.7 , pp. 297-307
    • Williams, K.J.1    Duncan, K.2
  • 4
    • 33751082642 scopus 로고    scopus 로고
    • Thymidylate synthase as a chemotherapeutic drug target: where are we after fifty years?
    • Berger F.G., and Berger S.H. Thymidylate synthase as a chemotherapeutic drug target: where are we after fifty years?. Cancer Biol. Ther. 5 (2006) 1238-1241
    • (2006) Cancer Biol. Ther. , vol.5 , pp. 1238-1241
    • Berger, F.G.1    Berger, S.H.2
  • 5
    • 13844298790 scopus 로고    scopus 로고
    • Targeting DHFR in parasitic protozoa
    • Anderson A.C. Targeting DHFR in parasitic protozoa. Drug Discov. Today 10 (2005) 121-128
    • (2005) Drug Discov. Today , vol.10 , pp. 121-128
    • Anderson, A.C.1
  • 6
    • 0035217760 scopus 로고    scopus 로고
    • The role of dUTPase and uracil-DNA repair in cancer chemotherapy
    • Ladner R.D. The role of dUTPase and uracil-DNA repair in cancer chemotherapy. Curr. Protein Pept. Sci. 2 (2001) 361-370
    • (2001) Curr. Protein Pept. Sci. , vol.2 , pp. 361-370
    • Ladner, R.D.1
  • 8
    • 0034744964 scopus 로고    scopus 로고
    • Homotrimeric dUTPases; structural solutions for specific recognition and hydrolysis of dUTP
    • Persson R., Cedergren-Zeppezauer E.S., and Wilson K.S. Homotrimeric dUTPases; structural solutions for specific recognition and hydrolysis of dUTP. Curr. Protein Pept. Sci. 2 (2001) 287-300
    • (2001) Curr. Protein Pept. Sci. , vol.2 , pp. 287-300
    • Persson, R.1    Cedergren-Zeppezauer, E.S.2    Wilson, K.S.3
  • 9
    • 38349191358 scopus 로고    scopus 로고
    • Mechanism of dTTP inhibition of the bifunctional dCTP deaminase:dUTPase encoded by Mycobacterium tuberculosis
    • Helt S.S., Thymark M., Harris P., Aagaard C., Dietrich J., Larsen S., and Willemoes M. Mechanism of dTTP inhibition of the bifunctional dCTP deaminase:dUTPase encoded by Mycobacterium tuberculosis. J. Mol. Biol. 376 (2008) 554-569
    • (2008) J. Mol. Biol. , vol.376 , pp. 554-569
    • Helt, S.S.1    Thymark, M.2    Harris, P.3    Aagaard, C.4    Dietrich, J.5    Larsen, S.6    Willemoes, M.7
  • 10
    • 0029882967 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP)
    • Larsson G., Svensson L.A., and Nyman P.O. Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP). Nat. Struct. Biol. 3 (1996) 532-538
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 532-538
    • Larsson, G.1    Svensson, L.A.2    Nyman, P.O.3
  • 14
    • 0025293893 scopus 로고
    • Protein sequence comparisons show that the 'pseudoproteases' encoded by poxviruses and certain retroviruses belong to the deoxyuridine triphosphatase family
    • McGeoch D.J. Protein sequence comparisons show that the 'pseudoproteases' encoded by poxviruses and certain retroviruses belong to the deoxyuridine triphosphatase family. Nucleic Acids Res. 18 (1990) 4105-4110
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4105-4110
    • McGeoch, D.J.1
  • 15
    • 5644258283 scopus 로고    scopus 로고
    • Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase
    • Barabas O., Pongracz V., Kovari J., Wilmanns M., and Vertessy B.G. Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase. J. Biol. Chem. 279 (2004) 42907-42915
    • (2004) J. Biol. Chem. , vol.279 , pp. 42907-42915
    • Barabas, O.1    Pongracz, V.2    Kovari, J.3    Wilmanns, M.4    Vertessy, B.G.5
  • 16
    • 36349007726 scopus 로고    scopus 로고
    • Kinetic mechanism of human dUTPase, an essential nucleotide pyrophosphatase enzyme
    • Toth J., Varga B., Kovacs M., Malnasi-Csizmadia A., and Vertessy B.G. Kinetic mechanism of human dUTPase, an essential nucleotide pyrophosphatase enzyme. J. Biol. Chem. 282 (2007) 33572-33582
    • (2007) J. Biol. Chem. , vol.282 , pp. 33572-33582
    • Toth, J.1    Varga, B.2    Kovacs, M.3    Malnasi-Csizmadia, A.4    Vertessy, B.G.5
  • 17
    • 0026684153 scopus 로고
    • A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems
    • Webb M.R. A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems. Proc. Natl. Acad. Sci. USA 89 (1992) 4884-4887
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4884-4887
    • Webb, M.R.1
  • 18
    • 45849087021 scopus 로고    scopus 로고
    • B. Varga, F. Migliardo, E. Takacs, G.B. Vertessy, S. Magazu, Experimental study on dUTPase-inhibitor candidate and dUTPase/disaccharide mixtures by PCS and ENS, J. Mol. Struct. (in press). Available online 9 November 2007.
    • B. Varga, F. Migliardo, E. Takacs, G.B. Vertessy, S. Magazu, Experimental study on dUTPase-inhibitor candidate and dUTPase/disaccharide mixtures by PCS and ENS, J. Mol. Struct. (in press). Available online 9 November 2007.
  • 19
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30 (1997) 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 20
    • 0028201833 scopus 로고
    • Identification of tyrosine as a functional residue in the active site of Escherichia coli dUTPase
    • Vertessy B.G., Zalud P., Nyman P.O., and Zeppezauer M. Identification of tyrosine as a functional residue in the active site of Escherichia coli dUTPase. Biochim. Biophys. Acta 1205 (1994) 146-150
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 146-150
    • Vertessy, B.G.1    Zalud, P.2    Nyman, P.O.3    Zeppezauer, M.4
  • 21
    • 0030755997 scopus 로고    scopus 로고
    • Flexible glycine rich motif of Escherichia coli deoxyuridine triphosphate nucleotidohydrolase is important for functional but not for structural integrity of the enzyme
    • Vertessy B.G. Flexible glycine rich motif of Escherichia coli deoxyuridine triphosphate nucleotidohydrolase is important for functional but not for structural integrity of the enzyme. Proteins 28 (1997) 568-579
    • (1997) Proteins , vol.28 , pp. 568-579
    • Vertessy, B.G.1
  • 22
    • 0032472214 scopus 로고    scopus 로고
    • The complete triphosphate moiety of non-hydrolyzable substrate analogues is required for a conformational shift of the flexible C-terminus in E. coli dUTP pyrophosphatase
    • Vertessy B.G., Larsson G., Persson T., Bergman A.C., Persson R., and Nyman P.O. The complete triphosphate moiety of non-hydrolyzable substrate analogues is required for a conformational shift of the flexible C-terminus in E. coli dUTP pyrophosphatase. FEBS Lett. 421 (1998) 83-88
    • (1998) FEBS Lett. , vol.421 , pp. 83-88
    • Vertessy, B.G.1    Larsson, G.2    Persson, T.3    Bergman, A.C.4    Persson, R.5    Nyman, P.O.6
  • 23
    • 0030587564 scopus 로고    scopus 로고
    • Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits
    • Mol C.D., Harris J.M., McIntosh E.M., and Tainer J.A. Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits. Structure 4 (1996) 1077-1092
    • (1996) Structure , vol.4 , pp. 1077-1092
    • Mol, C.D.1    Harris, J.M.2    McIntosh, E.M.3    Tainer, J.A.4
  • 25
    • 0029820083 scopus 로고    scopus 로고
    • Kinetic characterization of dUTPase from Escherichia coli
    • Larsson G., Nyman P.O., and Kvassman J.O. Kinetic characterization of dUTPase from Escherichia coli. J. Biol. Chem. 271 (1996) 24010-24016
    • (1996) J. Biol. Chem. , vol.271 , pp. 24010-24016
    • Larsson, G.1    Nyman, P.O.2    Kvassman, J.O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.