메뉴 건너뛰기




Volumn 1702, Issue 1, 2004, Pages 103-110

Esterase catalysis of substrate vapour: Enzyme activity occurs at very low hydration

Author keywords

Activity; Dynamics; Hydrolase; Lipase; Water

Indexed keywords

ESTERASE; LIPASE B; WATER;

EID: 4644278807     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.08.005     Document Type: Article
Times cited : (26)

References (53)
  • 1
    • 0025877453 scopus 로고
    • Protein hydration and function
    • J. Rupley, and G. Careri Protein hydration and function Adv. Protein Chem. 41 1991 37 172
    • (1991) Adv. Protein Chem. , vol.41 , pp. 37-172
    • Rupley, J.1    Careri, G.2
  • 2
    • 0033944466 scopus 로고    scopus 로고
    • Water in enzyme reactions: Biophysical aspects of hydration - dehydration processes
    • Y. Pocker Water in enzyme reactions: biophysical aspects of hydration - dehydration processes Cell. Mol. Life Sci. 57 2000 1008 1017
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1008-1017
    • Pocker, Y.1
  • 3
    • 0036205538 scopus 로고    scopus 로고
    • Water as it applies to the function of enzymes
    • J. Kornblatt, and M. Kornblatt Water as it applies to the function of enzymes Int. Rev. Cytol. 215 2002 49 73
    • (2002) Int. Rev. Cytol. , vol.215 , pp. 49-73
    • Kornblatt, J.1    Kornblatt, M.2
  • 4
    • 2342527858 scopus 로고    scopus 로고
    • Dynamics of water in biological recognition
    • S. Pal, and A. Zewail Dynamics of water in biological recognition Chem. Rev. 104 2004 2099 2123
    • (2004) Chem. Rev. , vol.104 , pp. 2099-2123
    • Pal, S.1    Zewail, A.2
  • 6
    • 0038057730 scopus 로고
    • Protein hydration
    • F. Franks The Humana Press New Jersey
    • F. Franks Protein hydration F. Franks Protein Biotechnology 1993 The Humana Press New Jersey 437 465
    • (1993) Protein Biotechnology , pp. 437-465
    • Franks, F.1
  • 7
    • 0018473089 scopus 로고
    • Lysozyme film hydration events: An IR and gravimetric study
    • G. Careri, A. Giansanti, and E. Gratton Lysozyme film hydration events: an IR and gravimetric study Biopolymers 18 1979 1187 1203
    • (1979) Biopolymers , vol.18 , pp. 1187-1203
    • Careri, G.1    Giansanti, A.2    Gratton, E.3
  • 8
    • 2742526640 scopus 로고    scopus 로고
    • Hydration processes in biological and macromolecular systems
    • J. Finney Hydration processes in biological and macromolecular systems Faraday Discuss. 103 1996 1 18
    • (1996) Faraday Discuss. , vol.103 , pp. 1-18
    • Finney, J.1
  • 9
    • 0018366224 scopus 로고
    • The effect of restricted hydration on the rate of reaction of glucose 6-phosphate dehydrogenase, phosphoglucose isomerase, hexokinase and fumarase
    • E. Stevens, and L. Stevens The effect of restricted hydration on the rate of reaction of glucose 6-phosphate dehydrogenase, phosphoglucose isomerase, hexokinase and fumarase Biochem. J. 179 1979 161 167
    • (1979) Biochem. J. , vol.179 , pp. 161-167
    • Stevens, E.1    Stevens, L.2
  • 10
    • 0003041627 scopus 로고
    • Enzyme activity as a function of water activity
    • D. Simatos J. Multon Martines Nijhoff Publishers Dordrecht
    • R. Drapron Enzyme activity as a function of water activity D. Simatos J. Multon Properties of Water in Foods 1985 Martines Nijhoff Publishers Dordrecht 171 190
    • (1985) Properties of Water in Foods , pp. 171-190
    • Drapron, R.1
  • 13
    • 0026547688 scopus 로고
    • Rhizomucor miehei lipase remains highly active at water activity below 0.0001
    • R. Valivety, P. Halling, and A. Macrae Rhizomucor miehei lipase remains highly active at water activity below 0.0001 FEBS Lett. 301 1992 258 260
    • (1992) FEBS Lett. , vol.301 , pp. 258-260
    • Valivety, R.1    Halling, P.2    MacRae, A.3
  • 14
    • 0024653016 scopus 로고
    • Enzymatic catalysis in anhydrous organic solvents
    • A. Klibanov Enzymatic catalysis in anhydrous organic solvents TIBS 14 1989 141 144
    • (1989) TIBS , vol.14 , pp. 141-144
    • Klibanov, A.1
  • 16
    • 0029560442 scopus 로고
    • Flexibility of enzymes suspended in organic solvents probed by time-resolved fluorescence anisotropy. Evidence that enzyme activity and enantioselectivity are directly related to enzyme flexibility
    • J. Broos, A. Visser, J. Engbersen, W. Verboom, A. van Hoek, and D. Reindoudt Flexibility of enzymes suspended in organic solvents probed by time-resolved fluorescence anisotropy. Evidence that enzyme activity and enantioselectivity are directly related to enzyme flexibility J. Am. Chem. Soc. 117 1995 12657 12663
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 12657-12663
    • Broos, J.1    Visser, A.2    Engbersen, J.3    Verboom, W.4    Van Hoek, A.5    Reindoudt, D.6
  • 17
    • 0001183512 scopus 로고
    • Structure and dynamics of cytochrome c in nonaqueous solvents by 2D NH-exchange NMR spectroscopy
    • J. Wu, and D. Gorenstein Structure and dynamics of cytochrome c in nonaqueous solvents by 2D NH-exchange NMR spectroscopy J. Am. Chem. Soc. 115 1993 6843 6850
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 6843-6850
    • Wu, J.1    Gorenstein, D.2
  • 18
    • 0022977879 scopus 로고
    • Enzyme technology and gas phase catalysis: Alcohol dehydrogenase example
    • S. Pulvin, M. Legoy, R. Lortie, M. Pensa, and D. Thomas Enzyme technology and gas phase catalysis: alcohol dehydrogenase example Biotechnol. Lett. 8 1986 783 784
    • (1986) Biotechnol. Lett. , vol.8 , pp. 783-784
    • Pulvin, S.1    Legoy, M.2    Lortie, R.3    Pensa, M.4    Thomas, D.5
  • 20
    • 0024764741 scopus 로고
    • Enzymatic oxidation of ethanol in the gaseous phase
    • E. Barzana, M. Karel, and A. Klibanov Enzymatic oxidation of ethanol in the gaseous phase Biotechnol. Bioeng. 34 1989 1178 1185
    • (1989) Biotechnol. Bioeng. , vol.34 , pp. 1178-1185
    • Barzana, E.1    Karel, M.2    Klibanov, A.3
  • 21
    • 0026816470 scopus 로고
    • Gas phase transesterification reactions catalyzed by lipolytic enzymes
    • F. Parvaresh, H. Robert, D. Thomas, and M.-D. Legoy Gas phase transesterification reactions catalyzed by lipolytic enzymes Biotechnol. Bioeng. 39 1992 467 473
    • (1992) Biotechnol. Bioeng. , vol.39 , pp. 467-473
    • Parvaresh, F.1    Robert, H.2    Thomas, D.3    Legoy, M.-D.4
  • 22
    • 0027321605 scopus 로고
    • Gas phase acetaldehyde production in a continuous bioreactor
    • S. Hwang, D. Trantolo, and D. Wise Gas phase acetaldehyde production in a continuous bioreactor Biotechnol. Bioeng. 42 1993 667 673
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 667-673
    • Hwang, S.1    Trantolo, D.2    Wise, D.3
  • 23
    • 0029636226 scopus 로고
    • Working at controlled water activity in a continuous process: The gas/solid system as a solution
    • S. Lamare, and M. Legoy Working at controlled water activity in a continuous process: the gas/solid system as a solution Biotechnol. Bioeng. 45 1995 387 397
    • (1995) Biotechnol. Bioeng. , vol.45 , pp. 387-397
    • Lamare, S.1    Legoy, M.2
  • 24
    • 0037023904 scopus 로고    scopus 로고
    • Direct transesterification of gases by "dry" immobilized lipase
    • P. Cameron, B. Davison, P. Frymier, and J. Barton Direct transesterification of gases by "dry" immobilized lipase Biotechnol. Bioeng. 78 2002 251 256
    • (2002) Biotechnol. Bioeng. , vol.78 , pp. 251-256
    • Cameron, P.1    Davison, B.2    Frymier, P.3    Barton, J.4
  • 25
    • 0037474265 scopus 로고    scopus 로고
    • Water plays a different role on activation thermodynamic parameters of alcoholysis reaction catalyzed by lipase in gaseous and organic media
    • M. Graber, M.-P. Bousquet-Dubouch, N. Sousa, S. Lamare, and M.-D. Legoy Water plays a different role on activation thermodynamic parameters of alcoholysis reaction catalyzed by lipase in gaseous and organic media Biochim. Biophys. Acta 1645 2003 56 62
    • (2003) Biochim. Biophys. Acta , vol.1645 , pp. 56-62
    • Graber, M.1    Bousquet-Dubouch, M.-P.2    Sousa, N.3    Lamare, S.4    Legoy, M.-D.5
  • 26
    • 0033400882 scopus 로고    scopus 로고
    • Supramolecular interactions of solid human serum albumin with binary mixtures of solvent vapors
    • V. Gorbatchuk, M. Ziganshin, and B. Solomonov Supramolecular interactions of solid human serum albumin with binary mixtures of solvent vapors Biophys. Chemist. 81 1999 107 123
    • (1999) Biophys. Chemist. , vol.81 , pp. 107-123
    • Gorbatchuk, V.1    Ziganshin, M.2    Solomonov, B.3
  • 27
    • 2342479757 scopus 로고    scopus 로고
    • Interaction enthalpies of solid human serum albumin with water - dioxane mixtures: Comparison with water and organic solvent vapor sorption
    • V. Sirotkin, and D. Faizullin Interaction enthalpies of solid human serum albumin with water - dioxane mixtures: comparison with water and organic solvent vapor sorption Thermochim. Acta 415 2004 127 133
    • (2004) Thermochim. Acta , vol.415 , pp. 127-133
    • Sirotkin, V.1    Faizullin, D.2
  • 28
    • 0001689772 scopus 로고
    • Protein hydration and enzyme activity: The role of hydration-induced conformation and dynamic changes in the activity of lysozyme
    • J. Finney, and P. Poole Protein hydration and enzyme activity: the role of hydration-induced conformation and dynamic changes in the activity of lysozyme Comments Mol. Cell. Biophys. 2 1984 129 151
    • (1984) Comments Mol. Cell. Biophys. , vol.2 , pp. 129-151
    • Finney, J.1    Poole, P.2
  • 30
    • 0019320989 scopus 로고
    • Correlation of IR spectroscopic, heat capacity, diagmagnetic susceptibility and enzymatic measurements on lysozyme powder
    • G. Careri, E. Gratton, P.-H. Yang, and J. Rupley Correlation of IR spectroscopic, heat capacity, diagmagnetic susceptibility and enzymatic measurements on lysozyme powder Nature 284 1980 572 573
    • (1980) Nature , vol.284 , pp. 572-573
    • Careri, G.1    Gratton, E.2    Yang, P.-H.3    Rupley, J.4
  • 31
    • 0018356110 scopus 로고
    • Protein - water interactions: Heat capacity of the lysozyme - water system
    • P.-H. Yang, and J. Rupley Protein - water interactions: heat capacity of the lysozyme - water system Biochemistry 18 1979 2654 2661
    • (1979) Biochemistry , vol.18 , pp. 2654-2661
    • Yang, P.-H.1    Rupley, J.2
  • 32
    • 0022425369 scopus 로고
    • Hydrogen exchange of lysozyme powders. Hydration dependence of internal motions
    • J. Schinkel, N. Downer, and J. Rupley Hydrogen exchange of lysozyme powders. Hydration dependence of internal motions Biochemistry 24 1985 352 366
    • (1985) Biochemistry , vol.24 , pp. 352-366
    • Schinkel, J.1    Downer, N.2    Rupley, J.3
  • 33
    • 0032147202 scopus 로고    scopus 로고
    • Role of water in plasticity, stability, and action of proteins: The crystal structures of lysozyme at very low levels of hydration
    • H. Nagendra, N. Sukumar, and M. Vijayan Role of water in plasticity, stability, and action of proteins: the crystal structures of lysozyme at very low levels of hydration Proteins 32 1998 229 240
    • (1998) Proteins , vol.32 , pp. 229-240
    • Nagendra, H.1    Sukumar, N.2    Vijayan, M.3
  • 34
    • 36149074059 scopus 로고
    • The control of humidity by saturated salt solutions
    • F. O'Brien The control of humidity by saturated salt solutions J. Sci. Instrum. 25 1948 73 76
    • (1948) J. Sci. Instrum. , vol.25 , pp. 73-76
    • O'Brien, F.1
  • 35
    • 0001749231 scopus 로고
    • Salts for static control of humidity at relatively low levels
    • G. Richardson, and R. Malthus Salts for static control of humidity at relatively low levels J. Appl. Chem. 5 1955 557 567
    • (1955) J. Appl. Chem. , vol.5 , pp. 557-567
    • Richardson, G.1    Malthus, R.2
  • 36
    • 0001124642 scopus 로고
    • Saturated salt solution for static control of relative humidities between 5°and 40 °C
    • L. Rockland Saturated salt solution for static control of relative humidities between 5°and 40 °C Anal. Chem. 32 1960 1375 1376
    • (1960) Anal. Chem. , vol.32 , pp. 1375-1376
    • Rockland, L.1
  • 38
    • 0022464520 scopus 로고
    • Solid-phase protein hydration studies
    • P. Poole, and J. Finney Solid-phase protein hydration studies Methods Enzymol. 127 1986 284 293
    • (1986) Methods Enzymol. , vol.127 , pp. 284-293
    • Poole, P.1    Finney, J.2
  • 40
    • 0028928260 scopus 로고
    • Enzyme memory. What is remembered and why?
    • A. Klibanov Enzyme memory. What is remembered and why? Nature 374 1995 596
    • (1995) Nature , vol.374 , pp. 596
    • Klibanov, A.1
  • 41
    • 1642372278 scopus 로고    scopus 로고
    • 2 activity in lipid monolayers is linked to interfacial water activity
    • 2 activity in lipid monolayers is linked to interfacial water activity Colloids Surf., B Biointerfaces 34 2004 197 204
    • (2004) Colloids Surf., B Biointerfaces , vol.34 , pp. 197-204
    • Rao, C.1    Damodaran, S.2
  • 43
    • 36849142809 scopus 로고
    • New looks at protein motions
    • H. Frauenfelder New looks at protein motions Nature 338 1989 623 624
    • (1989) Nature , vol.338 , pp. 623-624
    • Frauenfelder, H.1
  • 44
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • D. Koshland Application of a theory of enzyme specificity to protein synthesis Proc. Natl. Acad. Sci. U. S. A. 44 1958 98 105
    • (1958) Proc. Natl. Acad. Sci. U. S. A. , vol.44 , pp. 98-105
    • Koshland, D.1
  • 46
    • 84985676118 scopus 로고
    • Thermodynamic function of biopolymer hydration: I. Their determination by vapor pressure studies, discussed in an analysis of the primary hydration process
    • M. Lüscher-Mattli, and M. Rüegg Thermodynamic function of biopolymer hydration: I. Their determination by vapor pressure studies, discussed in an analysis of the primary hydration process Biopolymers 21 1982 403 418
    • (1982) Biopolymers , vol.21 , pp. 403-418
    • Lüscher-Mattli, M.1    Rüegg, M.2
  • 48
    • 4644243709 scopus 로고    scopus 로고
    • The use of gas-phase substrates to study enzyme catalysis at low hydration
    • in press.
    • R. Dunn, R. Daniel, The use of gas-phase substrates to study enzyme catalysis at low hydration, Phil. Trans. R. Soc. Lond. B, in press.
    • Phil. Trans. R. Soc. Lond. B
    • Dunn, R.1    Daniel, R.2
  • 50
    • 0034163362 scopus 로고    scopus 로고
    • Enzyme activity and dynamics: Xylanase activity in the absence of fast anharmonic dynamics
    • R. Dunn, V. Réat, J. Finney, M. Ferrand, J. Smith, and R. Daniel Enzyme activity and dynamics: xylanase activity in the absence of fast anharmonic dynamics Biochem. J. 346 2000 355 358
    • (2000) Biochem. J. , vol.346 , pp. 355-358
    • Dunn, R.1    Réat, V.2    Finney, J.3    Ferrand, M.4    Smith, J.5    Daniel, R.6
  • 52
    • 0032863425 scopus 로고    scopus 로고
    • Enzyme dynamics and activity: Time scale dependence of dynamical transition in glutamate dehydrogenase solution
    • R. Daniel, J. Finney, V. Reat, R. Dunn, M. Ferrand, and J. Smith Enzyme dynamics and activity: time scale dependence of dynamical transition in glutamate dehydrogenase solution Biophys. J. 77 1999 2184 2190
    • (1999) Biophys. J. , vol.77 , pp. 2184-2190
    • Daniel, R.1    Finney, J.2    Reat, V.3    Dunn, R.4    Ferrand, M.5    Smith, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.