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Volumn 417, Issue 1, 2011, Pages 136-141

Fluorescent substrate analog for monitoring chain elongation by undecaprenyl pyrophosphate synthase in real time

Author keywords

Fluorescent probe; Inhibitor; Isotope assay; Prenyltransferase; Single turnover

Indexed keywords

ESCHERICHIA COLI;

EID: 80655148686     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2011.05.043     Document Type: Article
Times cited : (10)

References (30)
  • 1
    • 0000680126 scopus 로고
    • Prenyl transferase and isomerase
    • S.L.R. Spurgeon (Ed.), Wiley, New York
    • C.D. Poulter, H.C. Rilling, Prenyl transferase and isomerase, in: S.L.R. Spurgeon (Ed.), Biosynthesis of Isoprenoid Compounds, vol. 1, Wiley, New York, 1981, pp. 161-224.
    • (1981) Biosynthesis of Isoprenoid Compounds , vol.1 , pp. 161-224
    • Poulter, C.D.1    Rilling, H.C.2
  • 3
    • 11544324496 scopus 로고    scopus 로고
    • Enzymatic aspects of isoprenoid chain elongation
    • K. Ogura, T. Koyama, Enzymatic aspects of isoprenoid chain elongation, Chem. Rev. 98 (1998) 1263-1276.
    • (1998) Chem. Rev. , vol.98 , pp. 1263-1276
    • Ogura, K.1    Koyama, T.2
  • 4
    • 0036375597 scopus 로고    scopus 로고
    • Structure, mechanism and function of prenyltransferases
    • DOI 10.1046/j.1432-1033.2002.03014.x
    • P.H. Liang, T.P. Ko, A.H. Wang, Structure, mechanism and function of prenyltransferases, Eur. J. Biochem. 269 (2002) 3339-3354. (Pubitemid 34988976)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.14 , pp. 3339-3354
    • Liang, P.-H.1    Ko, T.-P.2    Wang, A.H.-J.3
  • 5
    • 67650468659 scopus 로고    scopus 로고
    • Reaction kinetics, catalytic mechanisms, conformational changes, and inhibitor design for prenyltransferases
    • P.H. Liang, Reaction kinetics, catalytic mechanisms, conformational changes, and inhibitor design for prenyltransferases, Biochemistry 48 (2009) 6562- 6570.
    • (2009) Biochemistry , vol.48 , pp. 6562-6570
    • Liang, P.H.1
  • 6
    • 0032584588 scopus 로고    scopus 로고
    • Molecular cloning, expression, and purification of undecaprenyl diphosphate synthase. No sequence similarity between E- and Z-prenyl diphosphate synthases
    • DOI 10.1074/jbc.273.31.19476
    • N. Shimizu, T. Koyama, K. Ogura, Molecular cloning, expression, and purification of undecaprenyl diphosphate synthase. No sequence similarity between E- and Z-prenyl diphosphate synthases, J. Biol. Chem. 273 (1998) 19476-19481. (Pubitemid 28366997)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.31 , pp. 19476-19481
    • Shimizu, N.1    Koyama, T.2    Ogura, K.3
  • 7
    • 0345313624 scopus 로고    scopus 로고
    • Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: Cloning, expression, and characterization of the essential uppS gene
    • C.M. Apfel, B. Takacs, M. Fountoulakis, M. Stieger, W. Keck, Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: cloning, expression, and characterization of the essential uppS gene, J. Bacteriol. 181 (1999) 483-492. (Pubitemid 29045139)
    • (1999) Journal of Bacteriology , vol.181 , Issue.2 , pp. 483-492
    • Apfel, C.M.1    Takacs, B.2    Fountoulakis, M.3    Stieger, M.4    Keck, W.5
  • 9
    • 40749124827 scopus 로고    scopus 로고
    • Design and structure-activity relationships of potent and selective inhibitors of undecaprenyl pyrophosphate synthase (UPPS): Tetramic, tetronic acids and dihydropyridin-2-ones
    • DOI 10.1016/j.bmcl.2008.02.009, PII S0960894X08001893
    • S. Peukert, Y. Sun, R. Zhang, B. Hurley, M. Sabio, X. Shen, C. Gray, J. Dzink-Fox, J. Tao, R. Cebula, S. Wattanasin, Design and structure-activity relationships of potent and selective inhibitors of undecaprenyl pyrophosphate synthase (UPPS): tetramic, tetronic acids and dihydropyridin-2-ones, Bioorg. Med. Chem. Lett. 18 (2008) 1840-1844. (Pubitemid 351380899)
    • (2008) Bioorganic and Medicinal Chemistry Letters , vol.18 , Issue.6 , pp. 1840-1844
    • Peukert, S.1    Sun, Y.2    Zhang, R.3    Hurley, B.4    Sabio, M.5    Shen, X.6    Gray, C.7    Dzink-Fox, J.8    Tao, J.9    Cebula, R.10    Wattanasin, S.11
  • 10
    • 42949132874 scopus 로고    scopus 로고
    • Structure-based inhibitors exhibit differential activities against Helicobacter pylori and Escherichia coli undecaprenyl pyrophosphate synthases
    • C.J. Kuo, R.T. Guo, I.L. Lu, H.G. Liu, S.Y. Wu, T.P. Ko, A.H. Wang, P.H. Liang, Structure-based inhibitors exhibit differential activities against Helicobacter pylori and Escherichia coli undecaprenyl pyrophosphate synthases, J. Biomed. Biotechnol. 2008 (2008) 841312.
    • (2008) J. Biomed. Biotechnol. , vol.2008 , pp. 841312
    • Kuo, C.J.1    Guo, R.T.2    Lu, I.L.3    Liu, H.G.4    Wu, S.Y.5    Ko, T.P.6    Wang, A.H.7    Liang, P.H.8
  • 13
    • 0347298751 scopus 로고    scopus 로고
    • Synthesis and application of A fluorescent substrate analogue to study ligand interactions for undecaprenyl pyrophosphate synthase
    • DOI 10.1021/ja020937v
    • A.P. Chen, Y.H. Chen, H.P. Liu, Y.C. Li, C.T. Chen, P.H. Liang, Synthesis and application of a fluorescent substrate analogue to study ligand interactions for undecaprenyl pyrophosphate synthase, J. Am. Chem. Soc. 124 (2002) 15217- 15224. (Pubitemid 36014505)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.51 , pp. 15217-15224
    • Chen, A.P.-C.1    Chen, Y.-H.2    Liu, H.-P.3    Li, Y.-C.4    Chen, C.-T.5    Liang, P.-H.6
  • 15
    • 0034649372 scopus 로고    scopus 로고
    • Effect of site-directed mutagenesis of the conserved aspartate and glutamate on E. coli undecaprenyl pyrophosphate synthase catalysis
    • J.J. Pan, L.W. Yang, P.H. Liang, Effect of site-directed mutagenesis of the conserved aspartate and glutamate on E. coli undecaprenyl pyrophosphate synthase catalysis, Biochemistry 39 (2000) 13856-13861.
    • (2000) Biochemistry , vol.39 , pp. 13856-13861
    • Pan, J.J.1    Yang, L.W.2    Liang, P.H.3
  • 16
    • 0348111215 scopus 로고    scopus 로고
    • Identification of the Active Conformation and the Importance of Length of the Flexible Loop 72-83 in Regulating the Conformational Change of Undecaprenyl Pyrophosphate Synthase
    • DOI 10.1021/bi035283x
    • S.Y. Chang, Y.K. Chen, A.H. Wang, P.H. Liang, Identification of the active conformation and the importance of length of the flexible loop in regulating conformational change in undecaprenyl pyrophosphate synthase, Biochemistry 42 (2003) 14452-14459. (Pubitemid 37531990)
    • (2003) Biochemistry , vol.42 , Issue.49 , pp. 14452-14459
    • Chang, S.-Y.1    Chen, Y.-K.2    Wang, A.H.-J.3    Liang, P.-H.4
  • 19
    • 0030877321 scopus 로고    scopus 로고
    • Synthesis and evaluation of benzophenone-based photoaffinity labeling analogs of prenyl pyrophosphates containing stable amide linkages
    • DOI 10.1016/S0960-894X(97)00373-9, PII S0960894X97003739
    • T.C. Turek, I. Gaon, D. Gamache, M.D. Distefano, Synthesis and evaluation of benzophenone-based photoaffinity labeling analogs of prenyl pyrophosphates containing stable amide linkages, Bioorg. Med. Chem. Lett. 7 (1997) 2125-2130. (Pubitemid 27362117)
    • (1997) Bioorganic and Medicinal Chemistry Letters , vol.7 , Issue.16 , pp. 2125-2130
    • Turek, T.C.1    Gaon, I.2    Gamache, D.3    Distefano, M.D.4
  • 20
    • 0035906468 scopus 로고    scopus 로고
    • Synthesis of farnesyl diphosphate analogues containing ether-linked photoactive benzophenones and their application in studies of protein prenyltransferases
    • DOI 10.1021/jo991130x
    • T.C. Turek, I. Gaon, M.D. Distefano, C.L. Strickland, Synthesis of farnesyl diphosphate analogues containing ether-linked photoactive benzophenones and their application in studies of protein prenyltransferases, J. Org. Chem. 66 (2001) 3253-3264. (Pubitemid 32878931)
    • (2001) Journal of Organic Chemistry , vol.66 , Issue.10 , pp. 3253-3264
    • Turek, T.C.1    Gaon, I.2    Distefano, M.D.3
  • 22
    • 0034609518 scopus 로고    scopus 로고
    • Product distribution and pre-steady-state kinetic analysis of Escherichia coli undecaprenyl pyrophosphate synthase reaction
    • J.J. Pan, S.T. Chiou, P.H. Liang, Product distribution and pre-steady-state kinetic analysis of Escherichia coli undecaprenyl pyrophosphate synthase reaction, Biochemistry 39 (2000) 10936-10942.
    • (2000) Biochemistry , vol.39 , pp. 10936-10942
    • Pan, J.J.1    Chiou, S.T.2    Liang, P.H.3
  • 24
    • 0033718746 scopus 로고    scopus 로고
    • Theoretical studies of excited state proton transfer in small model systems
    • S. Scheiner, Theoretical studies of excited state proton transfer in small model systems, J. Phys. Chem. A 104 (2000) 5898.
    • (2000) J. Phys. Chem. A , vol.104 , pp. 5898
    • Scheiner, S.1
  • 25
    • 0018464261 scopus 로고
    • The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer
    • R.E. Dale, J. Eisinger, W.E. Blumberg, The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer, Biophys. J. 26 (1979) 161-193.
    • (1979) Biophys. J. , vol.26 , pp. 161-193
    • Dale, R.E.1    Eisinger, J.2    Blumberg, W.E.3
  • 28
    • 0037077666 scopus 로고    scopus 로고
    • A new type of excited-state intramolecular proton transfer: Proton transfer from phenol OH to a carbon atom of an aromatic ring observed for 2-phenylphenol
    • DOI 10.1021/ja0267831
    • M. Lukeman, P. Wan, A new type of excited-state intramolecular proton transfer: proton transfer from phenol OH to a carbon atom of an aromatic ring observed for 2-phenylphenol, J. Am. Chem. Soc. 124 (2002) 9458-9464. (Pubitemid 34856232)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.32 , pp. 9458-9464
    • Lukeman, M.1    Wan, P.2
  • 29
    • 0030561461 scopus 로고    scopus 로고
    • A spectrophotometric method to measure enzymatic activity in reactions that generate inorganic pyrophosphate
    • DOI 10.1006/abio.1996.0479
    • R.H. Upson, R.P. Haugland, M.N. Malekzadeh, A spectrophotometric method to measure enzymatic activity in reactions that generate inorganic pyrophosphate, Anal. Biochem. 243 (1996) 41-45. (Pubitemid 26418574)
    • (1996) Analytical Biochemistry , vol.243 , Issue.1 , pp. 41-45
    • Upson, R.H.1    Haugland, R.P.2    Malekzadeh, M.N.3    Haugland, R.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.