메뉴 건너뛰기




Volumn 77, Issue 1, 1999, Pages 85-98

Consequences of breaking the Asp-His hydrogen bond of the catalytic triad: Effects on the structure and dynamics of the serine esterase cutinase

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CUTINASE; GLYCINE; HISTIDINE; SERINE; SERINE PROTEINASE;

EID: 0032978685     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)76874-8     Document Type: Article
Times cited : (22)

References (48)
  • 2
    • 0030723218 scopus 로고    scopus 로고
    • A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment
    • Ash, E. L., J. L. Sudmeier, E. C. De Fabo, and W. W. Bachovchin. 1997. A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment. Science. 278:1128-1132.
    • (1997) Science , vol.278 , pp. 1128-1132
    • Ash, E.L.1    Sudmeier, J.L.2    De Fabo, E.C.3    Bachovchin, W.W.4
  • 4
    • 33947094423 scopus 로고
    • Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of α-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteases
    • Bachovchin, W. W., and J. D. Roberts. 1978. Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of α-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteases. J. Am. Chem. Soc. 100: 8041-8047.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 8041-8047
    • Bachovchin, W.W.1    Roberts, J.D.2
  • 5
    • 0014689979 scopus 로고
    • Role of a buried acid group in the mechanism of action of chymotrypsin
    • Blow, D. M., J. J. Birktoft, and B. S. Hartlet. 1969. Role of a buried acid group in the mechanism of action of chymotrypsin. Nature. 221: 337-340.
    • (1969) Nature , vol.221 , pp. 337-340
    • Blow, D.M.1    Birktoft, J.J.2    Hartlet, B.S.3
  • 8
    • 0016912106 scopus 로고
    • Some pertinent aspects of mechanisms as determined with small molecules
    • Bruice, T. C. 1976. Some pertinent aspects of mechanisms as determined with small molecules. Annu. Rev. Biochem. 45:331-373.
    • (1976) Annu. Rev. Biochem. , vol.45 , pp. 331-373
    • Bruice, T.C.1
  • 10
    • 0028030684 scopus 로고
    • Low-barrier hydrogen bonds and enzymatic catalysis
    • Cleland, W. W., and M. M. Kreevoy. 1994. Low-barrier hydrogen bonds and enzymatic catalysis. Science. 264:1887-1890.
    • (1994) Science , vol.264 , pp. 1887-1890
    • Cleland, W.W.1    Kreevoy, M.M.2
  • 12
    • 0031686334 scopus 로고    scopus 로고
    • Identification of functional and unfolding motions of cutinase as obtained from molecular dynamics computer simulations
    • Creveld, L. D., A. Amadei, R. C. van Schaik, H. A. M. Pepermans, J. de Vlieg, and H. J. C. Berendsen. 1998. Identification of functional and unfolding motions of cutinase as obtained from molecular dynamics computer simulations. Proteins. 33:253-264.
    • (1998) Proteins , vol.33 , pp. 253-264
    • Creveld, L.D.1    Amadei, A.2    Van Schaik, R.C.3    Pepermans, H.A.M.4    De Vlieg, J.5    Berendsen, H.J.C.6
  • 13
    • 0030768420 scopus 로고    scopus 로고
    • Structure as basis for understanding interfacial properties of lipases
    • Cygler, M., and J. D. Schrag. 1997. Structure as basis for understanding interfacial properties of lipases. Methods Enzymol. 284:3-27.
    • (1997) Methods Enzymol. , vol.284 , pp. 3-27
    • Cygler, M.1    Schrag, J.D.2
  • 14
    • 0015935205 scopus 로고
    • The charge relay system in chymotrypsin and chymotrypsinogen
    • Fersht, A. R., and J. Sperling. 1973. The charge relay system in chymotrypsin and chymotrypsinogen. J. Mol. Biol. 74:137-149.
    • (1973) J. Mol. Biol. , vol.74 , pp. 137-149
    • Fersht, A.R.1    Sperling, J.2
  • 15
    • 0028040716 scopus 로고
    • A tow-barrier hydrogen bond in the catalytic triad of serine proteases
    • Frey, P. A., S. A. Whitt, and J. B. Tobin. 1994. A tow-barrier hydrogen bond in the catalytic triad of serine proteases. Science. 264:1927-1930.
    • (1994) Science , vol.264 , pp. 1927-1930
    • Frey, P.A.1    Whitt, S.A.2    Tobin, J.B.3
  • 16
    • 0031127432 scopus 로고    scopus 로고
    • Understanding enzymatic catalysis: The importance of short, strong, hydrogen bonds
    • Geralt, J. A., M. M. Kreevoy, W. W. Cleland, and P. A. Frey. 1997. Understanding enzymatic catalysis: the importance of short, strong, hydrogen bonds. Chem. Biol. 4:259-267.
    • (1997) Chem. Biol. , vol.4 , pp. 259-267
    • Geralt, J.A.1    Kreevoy, M.M.2    Cleland, W.W.3    Frey, P.A.4
  • 17
    • 0030090490 scopus 로고    scopus 로고
    • Short strong hydrogen bonds: Can they explain enzymatic catalysis?
    • Guthrie, J. P. 1996. Short strong hydrogen bonds: can they explain enzymatic catalysis? Chem. Biol. 3:163-170.
    • (1996) Chem. Biol. , vol.3 , pp. 163-170
    • Guthrie, J.P.1
  • 18
    • 0026520387 scopus 로고
    • Converting trypsin to chymotrypsin: The role of surface loops
    • Hedstrom, L., L. Szilagyi, and W. J. Rutter. 1992. Converting trypsin to chymotrypsin: the role of surface loops. Science. 255:1249-1253.
    • (1992) Science , vol.255 , pp. 1249-1253
    • Hedstrom, L.1    Szilagyi, L.2    Rutter, W.J.3
  • 19
    • 0004014257 scopus 로고
    • Department of Biochemistry and Molecular Biology, University College, London
    • Hubbard, S. J., and J. M. Thornton. 1993. NACCESS. Department of Biochemistry and Molecular Biology, University College, London.
    • (1993) NACCESS
    • Hubbard, S.J.1    Thornton, J.M.2
  • 21
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein stuctures
    • Kraulis, P. J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein stuctures. J. Appl. Crystallogr. 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 22
    • 0017324044 scopus 로고
    • Serine proteases: Structure and mechanism of catalysis
    • Kraut, J. 1977. Serine proteases: structure and mechanism of catalysis. Annu. Rev. Biochem. 46:331-358.
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 331-358
    • Kraut, J.1
  • 23
    • 0032540681 scopus 로고    scopus 로고
    • - from 1,2-dichloroethane at the active site of Xanthobacter autotrophicus haloalkane dehalogenase
    • - from 1,2-dichloroethane at the active site of Xanthobacter autotrophicus haloalkane dehalogenase. J. Am. Chem. Soc. 120:5611-5621.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 5611-5621
    • Lightstone, F.C.1    Zheng, Y.-J.2    Bruice, T.C.3
  • 24
    • 0031574909 scopus 로고    scopus 로고
    • Atomic resolution (1.0 Å) crystal structure of Fusarium solani cutinase: Stereochemical analysis
    • Longhi, C. M., V. Lamzin, A. Nichols, and C. Cambillau. 1997. Atomic resolution (1.0 Å) crystal structure of Fusarium solani cutinase: stereochemical analysis. J. Mol. Biol. 268:779-799.
    • (1997) J. Mol. Biol. , vol.268 , pp. 779-799
    • Longhi, C.M.1    Lamzin, V.2    Nichols, A.3    Cambillau, C.4
  • 25
    • 0030470263 scopus 로고    scopus 로고
    • Dynamics of Fusarium solani cutinase investigated through structural comparisons among different crystal forms of its variants
    • Longhi, S., A. Nicolas, L. Creveld, M. Egmond, C. T. Verrips, J. de Vlieg, C. Martinez, and C. Cambillau. 1996. Dynamics of Fusarium solani cutinase investigated through structural comparisons among different crystal forms of its variants. Proteins. 26:442-458.
    • (1996) Proteins , vol.26 , pp. 442-458
    • Longhi, S.1    Nicolas, A.2    Creveld, L.3    Egmond, M.4    Verrips, C.T.5    De Vlieg, J.6    Martinez, C.7    Cambillau, C.8
  • 29
    • 0030041250 scopus 로고    scopus 로고
    • Contribution of cutinase serine 42 side-chain to the stabilization of the oxyanion transition state
    • Nicolas, A., M. Egmond, C. T. Verips, J. de Vlieg, S. Longhi, C. Cambillau, and C. Martinez. 1996. Contribution of cutinase serine 42 side-chain to the stabilization of the oxyanion transition state. Biochemistry. 35:398-410.
    • (1996) Biochemistry , vol.35 , pp. 398-410
    • Nicolas, A.1    Egmond, M.2    Verips, C.T.3    De Vlieg, J.4    Longhi, S.5    Cambillau, C.6    Martinez, C.7
  • 30
    • 0029939820 scopus 로고    scopus 로고
    • Effects of point mutants at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and function
    • Ohmae, E., K. Iriyama, S. Ichihara, and K. Gekko. 1996. Effects of point mutants at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and function. J. Biochem. 119:703-710.
    • (1996) J. Biochem. , vol.119 , pp. 703-710
    • Ohmae, E.1    Iriyama, K.2    Ichihara, S.3    Gekko, K.4
  • 31
    • 0029562951 scopus 로고
    • Molecular dynamics simulation of E. coli ribonuclease H1 in solution: Correlation with NMR and x-ray data and insights into biological function
    • Philippopoulos, M., and C. Lim. 1995. Molecular dynamics simulation of E. coli ribonuclease H1 in solution: correlation with NMR and x-ray data and insights into biological function. J. Mol. Biol. 254:771-792.
    • (1995) J. Mol. Biol. , vol.254 , pp. 771-792
    • Philippopoulos, M.1    Lim, C.2
  • 33
    • 0032558938 scopus 로고    scopus 로고
    • His-Asp catalytic dyad of ribonuclease A: Conformational stability of the wild-type, D121N, D121A, and H119A enzymes
    • Quirk, D. J., C. Park, J. E. Thompson, and R. T. Raines. 1998. His-Asp catalytic dyad of ribonuclease A: conformational stability of the wild-type, D121N, D121A, and H119A enzymes. Biochemistry. 37: 17958-17964.
    • (1998) Biochemistry , vol.37 , pp. 17958-17964
    • Quirk, D.J.1    Park, C.2    Thompson, J.E.3    Raines, R.T.4
  • 34
    • 0016395451 scopus 로고
    • Synthesis and evaluation of a model for the so-called "charge-relay" system of the serine esterase
    • Rogers, G. A., and T. C. Bruice. 1974. Synthesis and evaluation of a model for the so-called "charge-relay" system of the serine esterase. J. Am. Chem. Soc. 96:2473-2481.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 2473-2481
    • Rogers, G.A.1    Bruice, T.C.2
  • 35
    • 0032567157 scopus 로고    scopus 로고
    • Characterization of the short strong hydrogen bond in benzoylacetone by Ab initio calculations and accurate diffraction experiments. Implications for the electronic nature of low-barrier hydrogen bonds in enzymatic reactions
    • Schiott, B., B. B. Iversen, G. K. Hellerup Madsen, and T. C. Bruice. 1998. Characterization of the short strong hydrogen bond in benzoylacetone by Ab initio calculations and accurate diffraction experiments. Implications for the electronic nature of low-barrier hydrogen bonds in enzymatic reactions. J. Am. Chem. Soc. 120:12117-12124.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 12117-12124
    • Schiott, B.1    Iversen, B.B.2    Hellerup Madsen, G.K.3    Bruice, T.C.4
  • 36
    • 0030874881 scopus 로고    scopus 로고
    • Upases and α/β hydrolase fold
    • Schrag, J. D., and M. Cygler. 1997. Upases and α/β hydrolase fold. Methods Enzymol. 284:85-107.
    • (1997) Methods Enzymol. , vol.284 , pp. 85-107
    • Schrag, J.D.1    Cygler, M.2
  • 37
    • 0020020315 scopus 로고
    • Crystallographic and NMR studies of the serine proteases
    • Steitz, T. A., and R. G. Shulman. 1982. Crystallographic and NMR studies of the serine proteases. Annu. Rev. Biophys. Bioeng. 11:419-444.
    • (1982) Annu. Rev. Biophys. Bioeng. , vol.11 , pp. 419-444
    • Steitz, T.A.1    Shulman, R.G.2
  • 38
    • 0000118827 scopus 로고
    • Harmonic and quasiharmonic descriptions of crambin
    • Teeter, M. M., and D. A. Case. 1990. Harmonic and quasiharmonic descriptions of crambin. J. Phys. Chem. 94:8091-8097.
    • (1990) J. Phys. Chem. , vol.94 , pp. 8091-8097
    • Teeter, M.M.1    Case, D.A.2
  • 39
    • 22944467757 scopus 로고
    • Computer experiments on classical fluids
    • Verlet, L. 1967. Computer experiments on classical fluids. Phys. Rev. 159:98-113.
    • (1967) Phys. Rev. , vol.159 , pp. 98-113
    • Verlet, L.1
  • 40
    • 0031557394 scopus 로고    scopus 로고
    • Domain motions in dihydrofolate reductase: A molecular dynamics study
    • Verma, C. S., L. S. D. Caves, R. E. Hubbard, and G. C. K. Roberts. 1997. Domain motions in dihydrofolate reductase: a molecular dynamics study. J. Mol. Biol. 266:776-796.
    • (1997) J. Mol. Biol. , vol.266 , pp. 776-796
    • Verma, C.S.1    Caves, L.S.D.2    Hubbard, R.E.3    Roberts, G.C.K.4
  • 42
    • 0032538627 scopus 로고    scopus 로고
    • Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites
    • Warshel, A. 1998. Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites. J. Biol. Chem. 273: 27035-27038.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27035-27038
    • Warshel, A.1
  • 43
    • 0032568612 scopus 로고    scopus 로고
    • Computer simulations of enzyme catalysis: Finding out what has been optimized by nature
    • Warshel, A., and J. Florian. 1998. Computer simulations of enzyme catalysis: finding out what has been optimized by nature. Proc. Natl. Acad. Sci. USA. 95:5950-5955.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5950-5955
    • Warshel, A.1    Florian, J.2
  • 45
    • 0030462453 scopus 로고    scopus 로고
    • Energy considerations show that low-barrier hydrogen bonds do not offer a catalytic advantage over ordinary hydrogen bonds
    • Warshel, A., and A. Papazyan. 1996. Energy considerations show that low-barrier hydrogen bonds do not offer a catalytic advantage over ordinary hydrogen bonds. Proc. Natl. Acad. Sci. USA. 93:13665-13670.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13665-13670
    • Warshel, A.1    Papazyan, A.2
  • 46
    • 0029040169 scopus 로고
    • On low-barrier hydrogen bonds and enzyme catalysis
    • Warshel, A., A. Papazyan, and P. A. Kollman. 1995. On low-barrier hydrogen bonds and enzyme catalysis. Science. 269:102-104.
    • (1995) Science , vol.269 , pp. 102-104
    • Warshel, A.1    Papazyan, A.2    Kollman, P.A.3
  • 47
    • 0024278562 scopus 로고
    • Evaluation of catalytic free energies in genetically modified proteins
    • Warshel, A., F. Sussman, and J.-K. Hwang. 1988. Evaluation of catalytic free energies in genetically modified proteins. J. Mol. Biol. 201: 139-159.
    • (1988) J. Mol. Biol. , vol.201 , pp. 139-159
    • Warshel, A.1    Sussman, F.2    Hwang, J.-K.3
  • 48
    • 0000453071 scopus 로고
    • Importance of hydrogen-bond formation in stabilizing the transition state of subtilisin
    • Wells, J. A., B. C. Cunningham, T. P. Graycar, and D. A. Estell. 1986. Importance of hydrogen-bond formation in stabilizing the transition state of subtilisin. Philos. Trans. R. Soc. Lond. A. 317:415-423.
    • (1986) Philos. Trans. R. Soc. Lond. A. , vol.317 , pp. 415-423
    • Wells, J.A.1    Cunningham, B.C.2    Graycar, T.P.3    Estell, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.