메뉴 건너뛰기




Volumn 22, Issue 2, 2003, Pages 175-192

Hydrodynamic and spectroscopic studies of substrate binding to human recombinant deoxycytidine kinase

Author keywords

Circular dichroism; Deoxycytidine kinase; Fluorescence spectroscopy; Gemcitabine

Indexed keywords

ADENOSINE TRIPHOSPHATE; DEOXYCYTIDINE KINASE; GEMCITABINE; NUCLEOSIDE DERIVATIVE; RECOMBINANT ENZYME;

EID: 0242416537     PISSN: 15257770     EISSN: None     Source Type: Journal    
DOI: 10.1081/NCN-120019513     Document Type: Article
Times cited : (6)

References (34)
  • 1
    • 0030855683 scopus 로고    scopus 로고
    • Substrate specificity, expression, and primary sequences of deoxynucleoside kinases, implications for chemotherapy
    • Eriksson, S.; Wang, L. Substrate specificity, expression, and primary sequences of deoxynucleoside kinases, implications for chemotherapy. Nucleosides Nucleotides 1997, 16, 653-659.
    • (1997) Nucleosides Nucleotides , vol.16 , pp. 653-659
    • Eriksson, S.1    Wang, L.2
  • 2
    • 0030769662 scopus 로고    scopus 로고
    • The effects of high salt concentrations on the regulation of the substrate specificity of human recombinant deoxycytidine kinase
    • Usova, E.V.; Eriksson, S. The effects of high salt concentrations on the regulation of the substrate specificity of human recombinant deoxycytidine kinase. Eur. J. Biochem. 1997, 248, 762-766.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 762-766
    • Usova, E.V.1    Eriksson, S.2
  • 4
    • 0029162556 scopus 로고
    • Mammalian deoxyribonucleoside kinases
    • Arner, E.S.; Eriksson, S. Mammalian deoxyribonucleoside kinases. Pharmacol. Ther. 1995, 67, 155-186.
    • (1995) Pharmacol. Ther. , vol.67 , pp. 155-186
    • Arner, E.S.1    Eriksson, S.2
  • 5
    • 0027399054 scopus 로고
    • Cell cycle regulation of deoxycytidine kinase. Evidence for post-transcriptional control
    • Hengstschlager, M.; Denk, C.; Wawra, E. Cell cycle regulation of deoxycytidine kinase. Evidence for post-transcriptional control. FEBS Lett. 1993, 321, 237-240.
    • (1993) FEBS Lett. , vol.321 , pp. 237-240
    • Hengstschlager, M.1    Denk, C.2    Wawra, E.3
  • 6
    • 0030887265 scopus 로고    scopus 로고
    • Cloning of the cDNA and chromosome localization of the gene for human thymidine kinase 2
    • Johansson, M.; Karlsson, A. Cloning of the cDNA and chromosome localization of the gene for human thymidine kinase 2. J. Biol. Chem. 1997, 272, 8454-8458.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8454-8458
    • Johansson, M.1    Karlsson, A.2
  • 8
    • 0025878619 scopus 로고
    • A critical role for uridine nucleotides in the regulation of deoxycytidine kinase and the concentration dependence of 1-beta-D-arabinofuranosylcytosine phosphorylation in human leukemia cells
    • White, J.C.; Capizzi, R.L. A critical role for uridine nucleotides in the regulation of deoxycytidine kinase and the concentration dependence of 1-beta-D-arabinofuranosylcytosine phosphorylation in human leukemia cells. Cancer Res. 1991, 51, 2559-2565.
    • (1991) Cancer Res. , vol.51 , pp. 2559-2565
    • White, J.C.1    Capizzi, R.L.2
  • 9
    • 0027085703 scopus 로고
    • Nucleotide specificity of human deoxycytidine kinase
    • Shewach, D.S.; Reynolds, K.K.; Hertel, L. Nucleotide specificity of human deoxycytidine kinase. Mol. Pharmacol. 1992, 42, 518-524.
    • (1992) Mol. Pharmacol. , vol.42 , pp. 518-524
    • Shewach, D.S.1    Reynolds, K.K.2    Hertel, L.3
  • 10
    • 0028875580 scopus 로고
    • Nucleoside triphosphate donors for nucleoside kinases: Donor properties of UTP with human deoxycytidine kinase
    • Krawiec, K.; Kierdaszuk, B.; Eriksson, S.; Munch-Petersen, B.; Shugar, D. Nucleoside triphosphate donors for nucleoside kinases: donor properties of UTP with human deoxycytidine kinase. Biochem. Biophys. Res. Commun. 1995, 216, 42-48.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 42-48
    • Krawiec, K.1    Kierdaszuk, B.2    Eriksson, S.3    Munch-Petersen, B.4    Shugar, D.5
  • 11
    • 0014939576 scopus 로고
    • Deoxycytidine kinase. 3. Kinetics and allosteric regulation of the calf thymus enzyme
    • Ives, D. H.; Durham, J.P. Deoxycytidine kinase. 3. Kinetics and allosteric regulation of the calf thymus enzyme. J. Biol. Chem. 1970, 245, 2285-2294.
    • (1970) J. Biol. Chem. , vol.245 , pp. 2285-2294
    • Ives, D.H.1    Durham, J.P.2
  • 12
    • 0023919636 scopus 로고
    • Deoxycytidine kinase from human leukemic spleen: Preparation and characteristics of homogeneous enzyme
    • Bohman, C.; Eriksson, S. Deoxycytidine kinase from human leukemic spleen: preparation and characteristics of homogeneous enzyme. Biochemistry 1988, 27, 4258-4265.
    • (1988) Biochemistry , vol.27 , pp. 4258-4265
    • Bohman, C.1    Eriksson, S.2
  • 13
    • 0027505936 scopus 로고
    • Binding of substrates to human deoxycytidine kinase studied with ligand-dependent quenching of enzyme intrinsic fluorescence
    • Kierdaszuk, B.; Rigler, R.; Eriksson, S. Binding of substrates to human deoxycytidine kinase studied with ligand-dependent quenching of enzyme intrinsic fluorescence. Biochemistry 1993, 32, 699-707.
    • (1993) Biochemistry , vol.32 , pp. 699-707
    • Kierdaszuk, B.1    Rigler, R.2    Eriksson, S.3
  • 14
    • 0030977920 scopus 로고    scopus 로고
    • Kinetic analysis of human deoxycytidine kinase with the true phosphate donor uridine triphosphate
    • Hughes, T.L.; Hahn, T.M.; Reynolds, K.K.; Shewach, D.S. Kinetic analysis of human deoxycytidine kinase with the true phosphate donor uridine triphosphate. Biochemistry 1997, 36, 7540-7547.
    • (1997) Biochemistry , vol.36 , pp. 7540-7547
    • Hughes, T.L.1    Hahn, T.M.2    Reynolds, K.K.3    Shewach, D.S.4
  • 15
    • 0033614850 scopus 로고    scopus 로고
    • A pre-steady-state kinetic analysis of substrate binding to human recombinant deoxycytidine kinase: A model for nucleoside kinase action
    • Turk, B.; Awad, R.; Usova, E.V.; Bjork, I.; Eriksson, S. A pre-steady-state kinetic analysis of substrate binding to human recombinant deoxycytidine kinase: a model for nucleoside kinase action. Biochemistry 1999, 38, 8555-8561.
    • (1999) Biochemistry , vol.38 , pp. 8555-8561
    • Turk, B.1    Awad, R.2    Usova, E.V.3    Bjork, I.4    Eriksson, S.5
  • 16
    • 0014663430 scopus 로고
    • Measurement of protein concentration with interferences optics
    • Babul, J.; Stellwagen, E. Measurement of protein concentration with interferences optics. Anal. Biochem. 1969, 28, 216-221.
    • (1969) Anal. Biochem. , vol.28 , pp. 216-221
    • Babul, J.1    Stellwagen, E.2
  • 20
    • 0035980273 scopus 로고    scopus 로고
    • Physical Properties of Human Polynucleotide Kinase: Hydrodynamic and Spectroscopic Studies
    • Mani, R.S.; Karimi-Busheri, F.; Cass, C.E.; Weinfeld, M. Physical Properties of Human Polynucleotide Kinase: Hydrodynamic and Spectroscopic Studies. Biochemistry 2001, 40, 12967-12973.
    • (2001) Biochemistry , vol.40 , pp. 12967-12973
    • Mani, R.S.1    Karimi-Busheri, F.2    Cass, C.E.3    Weinfeld, M.4
  • 21
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • Johnson, M.L.; Correia, J.J.; Yphantis, D.A.; Halvorson, H.R. Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys. J. 1981, 36, 575-588.
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 22
    • 0242713195 scopus 로고
    • Cohn, E.J. Edsall, J.T., Eds.; Reinhold Publishing Corporation: New York, NY
    • Cohn, E.J.; Edsall, J.T. In Proteins, Cohn, E.J. Edsall, J.T., Eds.; Reinhold Publishing Corporation: New York, NY 1943.
    • (1943) Proteins
    • Cohn, E.J.1    Edsall, J.T.2
  • 23
    • 0025162271 scopus 로고
    • 2(+)-binding protein from smooth muscle
    • 2(+)-binding protein from smooth muscle. Biochemistry 1990, 29, 1398-1404.
    • (1990) Biochemistry , vol.29 , pp. 1398-1404
    • Mani, R.S.1    Kay, C.M.2
  • 24
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher, S.W.; Glöckner, J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 1981, 20, 33-37.
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glöckner, J.2
  • 26
    • 0015777319 scopus 로고
    • Ultraviolet difference spectroscopy-new techniques and applications
    • Donovan, J.W. Ultraviolet difference spectroscopy-new techniques and applications. Methods Enzymol. 1973, 27, 497-525.
    • (1973) Methods Enzymol. , vol.27 , pp. 497-525
    • Donovan, J.W.1
  • 27
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein, M.; Lesk, A.M.; Chothia, C. Structural mechanisms for domain movements in proteins. Biochemistry 1994, 33, 6739-6749.
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 28
    • 0029644168 scopus 로고    scopus 로고
    • Adenylate kinase motions during catalysis: An energetic counterweight balancing substrate binding
    • Muller, C.W.; Schlauderer, G.J.; Reinstein, J.; Schulz, G.E. Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding. Structure 1996, 4, 147-156.
    • (1996) Structure , vol.4 , pp. 147-156
    • Muller, C.W.1    Schlauderer, G.J.2    Reinstein, J.3    Schulz, G.E.4
  • 31
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: Implications for the mechanism of GTP hydrolysis
    • Pai, E.F.; Krengel, U.; Petsko, G.A.; Goody, R.S.; Kabsch, W.; Wittinghofer, A. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. Embo. J. 1990, 9, 2351-2359.
    • (1990) EMBO J. , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 32
    • 0027965652 scopus 로고
    • Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis
    • Coleman, D.E.; Berghuis, A.M.; Lee, E.; Linder, M.E.; Gilman, A.G.; Sprang, S.R. Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis. Science 1994, 265, 1405-1412.
    • (1994) Science , vol.265 , pp. 1405-1412
    • Coleman, D.E.1    Berghuis, A.M.2    Lee, E.3    Linder, M.E.4    Gilman, A.G.5    Sprang, S.R.6
  • 33
    • 0022971279 scopus 로고
    • Multisubstrate analogs for deoxynucleoside kinases. Triphosphate end products and synthetic bisubstrate analogs exhibit identical modes of binding and are useful probes for distinguishing kinetic mechanisms
    • Ikeda, S.; Chakravarty, R.; Ives, D.H. Multisubstrate analogs for deoxynucleoside kinases. Triphosphate end products and synthetic bisubstrate analogs exhibit identical modes of binding and are useful probes for distinguishing kinetic mechanisms. J. Biol. Chem. 1986, 261, 15,836-15,843.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15836-15843
    • Ikeda, S.1    Chakravarty, R.2    Ives, D.H.3
  • 34
    • 0033064944 scopus 로고    scopus 로고
    • Synthesis of new fluorescent nucleoside analogues and application to the study of human deoxycytidine kinase
    • Shafiee, M.; Gosselin, G.; Imbach, J.L.; Eriksson, S.; Maury, G. Synthesis of new fluorescent nucleoside analogues and application to the study of human deoxycytidine kinase. Nucleosides Nucleotides 1999, 18, 717-719.
    • (1999) Nucleosides Nucleotides , vol.18 , pp. 717-719
    • Shafiee, M.1    Gosselin, G.2    Imbach, J.L.3    Eriksson, S.4    Maury, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.