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Volumn 11, Issue 10, 2004, Pages 945-949

Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE KINASE;

EID: 4744343045     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb821     Document Type: Article
Times cited : (428)

References (28)
  • 1
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke, R. & Bohm, G. The stability of proteins in extreme environments. Curr. Opin. Struct Biol. 8, 738-748 (1998).
    • (1998) Curr. Opin. Struct Biol. , vol.8 , pp. 738-748
    • Jaenicke, R.1    Bohm, G.2
  • 2
    • 0034981542 scopus 로고    scopus 로고
    • Structural basis of thermostability in hyperthermophilic proteins, or "there's more than one way to skin a cat"
    • Petsko, G.A. Structural basis of thermostability in hyperthermophilic proteins, or "there's more than one way to skin a cat." Methods Enzymol. 334, 469-478 (2001).
    • (2001) Methods Enzymol. , vol.334 , pp. 469-478
    • Petsko, G.A.1
  • 3
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • Zavodszky, P., Kardos, J., Svingor & Petsko, G.A. Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. Proc. Natl. Acad. Sci. USA 95, 7406-7411 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7406-7411
    • Zavodszky, P.1    Kardos, J.2    Svingor3    Petsko, G.A.4
  • 4
    • 0037424370 scopus 로고    scopus 로고
    • Activity-stability relationships in extremophilic enzymes
    • D'Amico, S., Marx, J.C., Gerday, C. & Feller, G. Activity-stability relationships in extremophilic enzymes. J. Biol. Chem. 278, 7891-7896 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 7891-7896
    • D'Amico, S.1    Marx, J.C.2    Gerday, C.3    Feller, G.4
  • 5
    • 0033519723 scopus 로고    scopus 로고
    • Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase
    • Kohen, A., Cannio, R., Bartolucci, S. & Klinman, J.P. Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase. Nature 399, 496-499 (1999).
    • (1999) Nature , vol.399 , pp. 496-499
    • Kohen, A.1    Cannio, R.2    Bartolucci, S.3    Klinman, J.P.4
  • 6
    • 0029644728 scopus 로고
    • Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases
    • Vonrhein, C., Schlauderer, G.J. & Schulz, G.E. Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases. Structure 3, 483-490 (1995).
    • (1995) Structure , vol.3 , pp. 483-490
    • Vonrhein, C.1    Schlauderer, G.J.2    Schulz, G.E.3
  • 7
    • 0014429881 scopus 로고
    • Initial velocity and equilibrium kinetics of myokinase
    • Rhoads, D.G. & Lowenstein, J.M. Initial velocity and equilibrium kinetics of myokinase. J. Biol. Chem. 243, 3963-3972 (1968).
    • (1968) J. Biol. Chem. , vol.243 , pp. 3963-3972
    • Rhoads, D.G.1    Lowenstein, J.M.2
  • 8
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy
    • Loria, J.P., Rance, M. & Palmer, A.G. A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy. J. Am. Chem. Soc. 121, 2331-2332 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer, A.G.3
  • 10
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
    • Palmer, A.G., Kroenke, C.D. & Loria, J.P. Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules, Methods Enzymol. 339, 204-238 (2001).
    • (2001) Methods Enzymol. , vol.339 , pp. 204-238
    • Palmer, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 11
    • 0040362704 scopus 로고    scopus 로고
    • Chemical basis for enzyme catalysis
    • Bruice, T.C. & Benkovic, S.J. Chemical basis for enzyme catalysis. Biochemistry 39, 5267-6274 (2000).
    • (2000) Biochemistry , vol.39 , pp. 5267-6274
    • Bruice, T.C.1    Benkovic, S.J.2
  • 14
    • 0026544877 scopus 로고
    • Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 Å resolution. A model for a catalytic transition state
    • Muller, C.W. & Schulz, G.E. Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 Å resolution. A model for a catalytic transition state. J. Mol. Biol. 224, 159-177 (1992).
    • (1992) J. Mol. Biol. , vol.224 , pp. 159-177
    • Muller, C.W.1    Schulz, G.E.2
  • 15
    • 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. Structured, 147-156 (1996).
    • (1996) Structured , pp. 147-156
    • Muller, C.W.1    Schlauderer, G.J.2    Reinstein, J.3    Schulz, G.E.4
  • 16
    • 0028338283 scopus 로고
    • The closed conformation of a highly flexible protein: The structure of E. coli adenylate kinase with bound AMP and AMPPNP
    • Berry, M.B. et al. The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP. Proteins 19, 183-198 (1994).
    • (1994) Proteins , vol.19 , pp. 183-198
    • Berry, M.B.1
  • 17
    • 0035967856 scopus 로고    scopus 로고
    • Solution-state NMR investigations of triosephosphate isomerase active site loop motion: Ligand release in relation to active site loop dynamics
    • Rozovsky, S., Jogl, G., Tong, L. & McDermott, A.E. Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics. J. Mol. Biol. 310, 271-280 (2001).
    • (2001) J. Mol. Biol. , vol.310 , pp. 271-280
    • Rozovsky, S.1    Jogl, G.2    Tong, L.3    McDermott, A.E.4
  • 18
    • 0035928796 scopus 로고    scopus 로고
    • Backbone dynamics in dihydrofolate reductase complexes: Role of loop flexibility in the catalytic mechanism
    • Osborne, M.J., Schnell, J., Benkovic, S.J., Dyson, H.J. & Wright, P.E. Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism. Biochemistry 40, 9846-9859 (2001).
    • (2001) Biochemistry , vol.40 , pp. 9846-9859
    • Osborne, M.J.1    Schnell, J.2    Benkovic, S.J.3    Dyson, H.J.4    Wright, P.E.5
  • 19
    • 0028921302 scopus 로고
    • Flexibility and function in HIV-1 protease
    • Nicholson, L.K. et al. Flexibility and function in HIV-1 protease. Nat. Struct. Biol. 2, 274-280 (1995).
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 274-280
    • Nicholson, L.K.1
  • 20
    • 0034945906 scopus 로고    scopus 로고
    • Functional dynamics in the active site of the ribonuclease binase
    • Wang, L. et al. Functional dynamics in the active site of the ribonuclease binase. Proc. Natl. Acad. Sci. USA 98, 7684-7689 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7684-7689
    • Wang, L.1
  • 22
    • 0024298856 scopus 로고
    • Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli
    • Reinstein, J., Brune, M. & Wittinghofer, A. Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli. Biochemistry 27, 4712-4720 (1988).
    • (1988) Biochemistry , vol.27 , pp. 4712-4720
    • Reinstein, J.1    Brune, M.2    Wittinghofer, A.3
  • 23
    • 0032612062 scopus 로고    scopus 로고
    • 1H, 13C and 15N backbone resonance assignment of Escherichia coli adenylate kinase, a 23.6 kDa protein
    • Burlacu-Miron, S. et al. 1H, 13C and 15N backbone resonance assignment of Escherichia coli adenylate kinase, a 23.6 kDa protein. J. Biomol. NMR 13, 93-94 (1999).
    • (1999) J. Biomol. NMR , vol.13 , pp. 93-94
    • Burlacu-Miron, S.1
  • 25
    • 0002889918 scopus 로고
    • A general two-site solution for the chemical exchange produced dependence of T2 upon the Carr-Purcell pulse separation
    • Carver, J.P. & Richards, R.E. A general two-site solution for the chemical exchange produced dependence of T2 upon the Carr-Purcell pulse separation. J. Magn. Reson. 6, 89-105 (1972).
    • (1972) J. Magn. Reson. , vol.6 , pp. 89-105
    • Carver, J.P.1    Richards, R.E.2
  • 26
    • 0034728579 scopus 로고    scopus 로고
    • The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale
    • Millet, O., Loria, J.P., Kroenke, C.D., Rons, M. & Palmer, A.G. The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale. J. Am. Chem. Soc. 122, 2867-2877 (2000).
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2867-2877
    • Millet, O.1    Loria, J.P.2    Kroenke, C.D.3    Rons, M.4    Palmer, A.G.5
  • 27
    • 0001303793 scopus 로고
    • A unified theory of exchange effects on nuclear magnetic resonance line shapes
    • Binsch, G. A unified theory of exchange effects on nuclear magnetic resonance line shapes. J. Am. Chem. Soc. 91, 1304-1309 (1969).
    • (1969) J. Am. Chem. Soc. , vol.91 , pp. 1304-1309
    • Binsch, G.1
  • 28
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. & Wuthrich, K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55, 29-32 (1996).
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.