메뉴 건너뛰기




Volumn 264, Issue 2, 1999, Pages 327-335

Differential effect of pressure and temperature on the catalytic behaviour of wild-type human butyrylcholinesterase and its D70g mutant

Author keywords

Arrhenius plot; Butyrylcholinesterase; Pressure; Temperature; Van't Hoff plot

Indexed keywords

CHOLINESTERASE; MUTANT PROTEIN;

EID: 0033199559     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00609.x     Document Type: Article
Times cited : (10)

References (52)
  • 1
    • 33845282579 scopus 로고
    • Acetylcholinesterase: Enzyme structure, reaction dynamics, and virtual transition states
    • Quinn, D.M. (1987) Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states. Chem. Rev. 87, 955-979.
    • (1987) Chem. Rev. , vol.87 , pp. 955-979
    • Quinn, D.M.1
  • 3
    • 0025294717 scopus 로고
    • Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine
    • Lockridge, O. (1990) Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine. Pharmacol. Ther. 47, 35-60.
    • (1990) Pharmacol. Ther. , vol.47 , pp. 35-60
    • Lockridge, O.1
  • 4
    • 0032488593 scopus 로고    scopus 로고
    • Organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase: Synergy results in a somanase
    • Millard, C.B., Lockridge, O. & Broomfield, C.A. (1998) Organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase: synergy results in a somanase. Biochemistry 37(1), 237-247.
    • (1998) Biochemistry , vol.37 , Issue.1 , pp. 237-247
    • Millard, C.B.1    Lockridge, O.2    Broomfield, C.A.3
  • 5
    • 0000416402 scopus 로고
    • The activity of various esterase inhibitors towards atypical human serum cholinesterase
    • Kalow, W. & Davies, R.O. (1958) The activity of various esterase inhibitors towards atypical human serum cholinesterase. Biochem. Pharmacol. 1, 183-192.
    • (1958) Biochem. Pharmacol. , vol.1 , pp. 183-192
    • Kalow, W.1    Davies, R.O.2
  • 7
    • 0025610229 scopus 로고
    • Anionic site interactions in human butyrylcholinesterase disrupted by two single point mutations
    • Neville, L.F., Gnatt, A., Padan, R., Seidman, S. & Soreq, H. (1990) Anionic site interactions in human butyrylcholinesterase disrupted by two single point mutations. J. Biol. Chem. 265, 20735-30738.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20735-30738
    • Neville, L.F.1    Gnatt, A.2    Padan, R.3    Seidman, S.4    Soreq, H.5
  • 8
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman, J.L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L. & Silman, I. (1991) Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 253, 872-879.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 10
    • 0029665127 scopus 로고    scopus 로고
    • Asp70 in the peripheral anionic site of human butyrylcholinesterase
    • Masson, P., Froment, M.T., Bartels, C.F. & Lockridge, O. (1996) Asp70 in the peripheral anionic site of human butyrylcholinesterase. Eur. J. Biochem. 235, 36-48.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 36-48
    • Masson, P.1    Froment, M.T.2    Bartels, C.F.3    Lockridge, O.4
  • 11
    • 0030668464 scopus 로고    scopus 로고
    • Tetramerization domain of human butyrylcholinesterase is at the C-terminus
    • Blong, R.M., Bedows, E. & Lockridge, O. (1997) Tetramerization domain of human butyrylcholinesterase is at the C-terminus. Biochem. J. 327, 747-757.
    • (1997) Biochem. J. , vol.327 , pp. 747-757
    • Blong, R.M.1    Bedows, E.2    Lockridge, O.3
  • 12
    • 0032476586 scopus 로고    scopus 로고
    • A four-to-one association between peptide motifs: Four C-terminal domains from cholinesterase assemble with one proline-rich attachment domain (PRAD) in the secretory pathway
    • Simon, S., Krejci, E. & Massoulié, J. (1998) A four-to-one association between peptide motifs: four C-terminal domains from cholinesterase assemble with one proline-rich attachment domain (PRAD) in the secretory pathway. EMBO J. 17, 6178-6187.
    • (1998) EMBO J. , vol.17 , pp. 6178-6187
    • Simon, S.1    Krejci, E.2    Massoulié, J.3
  • 13
    • 0031043533 scopus 로고    scopus 로고
    • Role of aspartate 70 and tryptophan 82 in binding of succinyldithiocholine to human butyrylcholinesterase
    • Masson, P., Legrand, P., Bartels, C.F., Froment, M.T., Schopfer, L.M. & Lockridge, O. (1997) Role of aspartate 70 and tryptophan 82 in binding of succinyldithiocholine to human butyrylcholinesterase. Biochemistry 36, 2266-2277.
    • (1997) Biochemistry , vol.36 , pp. 2266-2277
    • Masson, P.1    Legrand, P.2    Bartels, C.F.3    Froment, M.T.4    Schopfer, L.M.5    Lockridge, O.6
  • 15
    • 0018793465 scopus 로고
    • A mechanistic model for butyrylcholinesterase
    • Eriksson, H. & Augustinsson, K.B. (1979) A mechanistic model for butyrylcholinesterase. Biochim. Biophys. Acta 567, 161-173.
    • (1979) Biochim. Biophys. Acta , vol.567 , pp. 161-173
    • Eriksson, H.1    Augustinsson, K.B.2
  • 16
    • 0023605724 scopus 로고
    • Horse serum butyrylcholinesterase kinetics: A molecular mechanism based on inhibition studies with dansylaminoethyltrimethylammonium
    • Cauet, G., Friboulet, A. & Thomas, D. (1987) Horse serum butyrylcholinesterase kinetics: a molecular mechanism based on inhibition studies with dansylaminoethyltrimethylammonium. Biochem. Cell. Biol. 65, 529-535.
    • (1987) Biochem. Cell. Biol. , vol.65 , pp. 529-535
    • Cauet, G.1    Friboulet, A.2    Thomas, D.3
  • 17
    • 0032946621 scopus 로고    scopus 로고
    • Polyol-induced activation by excess substrate of the D70G butyrylcholinesterase mutant
    • Levitsky, V., Xie, W., Froment, M.T., Lockridge, O. & Masson, P. (1999) Polyol-induced activation by excess substrate of the D70G butyrylcholinesterase mutant. Biochim. Biophys. Acta 1429, 422-430.
    • (1999) Biochim. Biophys. Acta , vol.1429 , pp. 422-430
    • Levitsky, V.1    Xie, W.2    Froment, M.T.3    Lockridge, O.4    Masson, P.5
  • 18
    • 0023007922 scopus 로고
    • Thermodynamic arguments for temperature-induced cryptic conformational change of human plasma cholinesterase
    • Masson, P. & Balny, C. (1986) Thermodynamic arguments for temperature-induced cryptic conformational change of human plasma cholinesterase. Biochim. Biophys. Acta 874, 90-98.
    • (1986) Biochim. Biophys. Acta , vol.874 , pp. 90-98
    • Masson, P.1    Balny, C.2
  • 19
    • 0023241821 scopus 로고
    • Kinetic evidence for thermally induced conformational change of butyrylcholinesterase
    • Ferro, A. & Masson, P. (1987) Kinetic evidence for thermally induced conformational change of butyrylcholinesterase, Biochim. Biophys. Acta 916, 193-199.
    • (1987) Biochim. Biophys. Acta , vol.916 , pp. 193-199
    • Ferro, A.1    Masson, P.2
  • 20
    • 0026662384 scopus 로고
    • Soman inhibition of butyrylcholinesterase in the presence of substrate: Pressure and temperature perturbations
    • Cléry, C., Massen, P., Heiber-Langer, I. & Balny, C. (1992) Soman inhibition of butyrylcholinesterase in the presence of substrate: pressure and temperature perturbations. Biochim. Biophys. Acta 1159, 295-302.
    • (1992) Biochim. Biophys. Acta , vol.1159 , pp. 295-302
    • Cléry, C.1    Massen, P.2    Heiber-Langer, I.3    Balny, C.4
  • 21
    • 0027273738 scopus 로고
    • Recombinant human butyrylcholinesterase G390V, the fluoride-2 variant, expressed in Chinese hamster ovary cells, is a low affinity variant
    • Masson, P., Adkins, S., Gouet, P. & Lockridge, O. (1993) Recombinant human butyrylcholinesterase G390V, the fluoride-2 variant, expressed in Chinese hamster ovary cells, is a low affinity variant. J. Biol. Chem. 268(19), 14329-14341.
    • (1993) J. Biol. Chem. , vol.268 , Issue.19 , pp. 14329-14341
    • Masson, P.1    Adkins, S.2    Gouet, P.3    Lockridge, O.4
  • 22
    • 0019484519 scopus 로고
    • The theory of pressure effects on enzymes
    • Moríld, E. (198I) The theory of pressure effects on enzymes. Adv. Protein Chem. 34, 93-166.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 93-166
    • Moríld, E.1
  • 23
    • 0020017199 scopus 로고
    • High pressure effects on proteins and other biomolecules
    • Heremans, K. (1982) High pressure effects on proteins and other biomolecules. Annu. Rev. Biophys. 11, 1-21.
    • (1982) Annu. Rev. Biophys. , vol.11 , pp. 1-21
    • Heremans, K.1
  • 24
    • 0024067935 scopus 로고
    • High pressure studies of enzyme catalysis
    • Taniguchi, Y. & Makimoto, S. (1988) High pressure studies of enzyme catalysis. J. Mol. Catal. 47, 323-324.
    • (1988) J. Mol. Catal. , vol.47 , pp. 323-324
    • Taniguchi, Y.1    Makimoto, S.2
  • 25
    • 84963456797 scopus 로고
    • Some recent aspects of the use of high-pressure for protein investigations in solution
    • Balny, C., Masson, P. & Travers, F. (1989) Some recent aspects of the use of high-pressure for protein investigations in solution. High Pressure Res. 1-28.
    • (1989) High Pressure Res. , pp. 1-28
    • Balny, C.1    Masson, P.2    Travers, F.3
  • 26
    • 0028220701 scopus 로고
    • The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes
    • Gross, M. & Jaenicke, R. (1994) The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur. J. Biochem. 221, 617-630.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 617-630
    • Gross, M.1    Jaenicke, R.2
  • 27
    • 0030065265 scopus 로고    scopus 로고
    • High pressure effects on protein structure and function
    • Mozhaev, V.V., Heremans, K., Frank, J., Masson, P. & Balny, C. (1996) High pressure effects on protein structure and function. Proteins 24, 81-91.
    • (1996) Proteins , vol.24 , pp. 81-91
    • Mozhaev, V.V.1    Heremans, K.2    Frank, J.3    Masson, P.4    Balny, C.5
  • 28
    • 0015105674 scopus 로고
    • The anomalous temperature dependence of enzyme-catalyzed reactions
    • Talsky, G. (1971) The anomalous temperature dependence of enzyme-catalyzed reactions. Angew. Chem. Int. Ed. Engl. 10, 549-555.
    • (1971) Angew. Chem. Int. Ed. Engl. , vol.10 , pp. 549-555
    • Talsky, G.1
  • 29
    • 0017857866 scopus 로고
    • Effect of high pressure, detergents and phospholipase on the break in the Arrhenius plot of Azotobacter nitrogenase
    • Ceuterick, F., Peeters, J., Heremans, K., De Smedt, H. & Olbrechts, H. (1978) Effect of high pressure, detergents and phospholipase on the break in the Arrhenius plot of Azotobacter nitrogenase. Eur. J. Biochem. 87, 401-408.
    • (1978) Eur. J. Biochem. , vol.87 , pp. 401-408
    • Ceuterick, F.1    Peeters, J.2    Heremans, K.3    De Smedt, H.4    Olbrechts, H.5
  • 31
    • 0019322409 scopus 로고
    • 2+-ATPase from sarcoplasmic reticulum
    • 2+-ATPase from sarcoplasmic reticulum. FEBS Lett. 1117(1), 161-163.
    • (1980) FEBS Lett. , vol.1117 , Issue.1 , pp. 161-163
    • Heremans, K.1    Wuytack, F.2
  • 32
    • 0009674331 scopus 로고
    • Pressure effects on protein-lipid interactions
    • Heremans, K., De Smedt, H. & Wuytack, F. (1982) Pressure effects on protein-lipid interactions. Biophys. J. 37, 74-75.
    • (1982) Biophys. J. , vol.37 , pp. 74-75
    • Heremans, K.1    De Smedt, H.2    Wuytack, F.3
  • 33
    • 0019000671 scopus 로고
    • The causes of sharply bent or discontinuous Arrhenius plots for enzyme-catalysed reactions
    • Londesborough, J. (1980) The causes of sharply bent or discontinuous Arrhenius plots for enzyme-catalysed reactions. Eur. J. Biochem. 105, 211-215.
    • (1980) Eur. J. Biochem. , vol.105 , pp. 211-215
    • Londesborough, J.1
  • 34
    • 0028886045 scopus 로고
    • Kinetics of butyrylcholinesterase in reversed micelles under high pressure
    • Cléry, C., Bec, N., Balny, C., Mozhaev, V.V. & Masson, P. (1995) Kinetics of butyrylcholinesterase in reversed micelles under high pressure. Biochim. Biophys. Acta 1253, 85-93.
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 85-93
    • Cléry, C.1    Bec, N.2    Balny, C.3    Mozhaev, V.V.4    Masson, P.5
  • 35
  • 36
    • 0000748473 scopus 로고
    • Pressure dependence of weak acid ionization in aqueous buffers
    • Neuman, R.C., Kauzmann, W. & Zipp, A. (1973) Pressure dependence of weak acid ionization in aqueous buffers. J. Phys. Chem. 77, 2687-2691.
    • (1973) J. Phys. Chem. , vol.77 , pp. 2687-2691
    • Neuman, R.C.1    Kauzmann, W.2    Zipp, A.3
  • 38
    • 0014208247 scopus 로고
    • The inhibitory effect of Tris on the activity of cholinesterases
    • Pavlic, M. (1967) The inhibitory effect of Tris on the activity of cholinesterases. Biochim. Biophys. Acta 139, 133-137.
    • (1967) Biochim. Biophys. Acta , vol.139 , pp. 133-137
    • Pavlic, M.1
  • 39
    • 0027517144 scopus 로고
    • Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors
    • Radic, Z., Pickering, N.A., Vellom, D.C., Camp, S. & Taylor, P. (1993) Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors. Biochemistry 32, 12074-12084.
    • (1993) Biochemistry , vol.32 , pp. 12074-12084
    • Radic, Z.1    Pickering, N.A.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 40
    • 0023193524 scopus 로고
    • Substrate activation and thermal denaturation kinetics of the tetrameric and the trypsin-generated monomeric forms of horse serum butyrylcholinesterase
    • Cauet, G., Friboulet, A. & Thomas, D. (1987) Substrate activation and thermal denaturation kinetics of the tetrameric and the trypsin-generated monomeric forms of horse serum butyrylcholinesterase. Biochim. Biophys. Acta 912, 338-342.
    • (1987) Biochim. Biophys. Acta , vol.912 , pp. 338-342
    • Cauet, G.1    Friboulet, A.2    Thomas, D.3
  • 41
    • 0025202704 scopus 로고
    • Conformational plasticity of butyrylcholinesterase as revealed by high pressure experiments
    • Masson, P. & Balny, C. (1990) Conformational plasticity of butyrylcholinesterase as revealed by high pressure experiments. Biochim. Biophys. Acta 1041, 223-231.
    • (1990) Biochim. Biophys. Acta , vol.1041 , pp. 223-231
    • Masson, P.1    Balny, C.2
  • 42
    • 0028356702 scopus 로고
    • Pressure and propylene carbonate denaturation of native and 'aged' phosphorylated cholinesterase
    • Masson, P., Gouet, P. & Cléry, C. (1994) Pressure and propylene carbonate denaturation of native and 'aged' phosphorylated cholinesterase. J. Mol. Biol. 238, 466-478.
    • (1994) J. Mol. Biol. , vol.238 , pp. 466-478
    • Masson, P.1    Gouet, P.2    Cléry, C.3
  • 43
    • 0033029009 scopus 로고    scopus 로고
    • Structural and hydration changes in the active site gorge of phosphylated butyrylcholinesterase (BuChE) accompanying the aging process
    • Masson, P., Fortier, P.L., Albaret, C., Cléry, C., Guerra, P. & Lockridge, O. (1999) Structural and hydration changes in the active site gorge of phosphylated butyrylcholinesterase (BuChE) accompanying the aging process. Chem. Biol. Interact. 119-120, 17-27.
    • (1999) Chem. Biol. Interact. , vol.119-120 , pp. 17-27
    • Masson, P.1    Fortier, P.L.2    Albaret, C.3    Cléry, C.4    Guerra, P.5    Lockridge, O.6
  • 44
    • 0001753330 scopus 로고
    • Acetylcholinesterase: Enthalpies and entropies of activation
    • Wilson, I.E. &Cabib, E. (1956) Acetylcholinesterase: enthalpies and entropies of activation. J. Am. Chem. Soc. 78, 202-207.
    • (1956) J. Am. Chem. Soc. , vol.78 , pp. 202-207
    • Wilson, I.E.1    Cabib, E.2
  • 45
    • 0029133160 scopus 로고
    • Pressure-induced molten globule state of cholinesterase
    • Cléry, C., Renault, F. & Masson, P. (1995) Pressure-induced molten globule state of cholinesterase. FEBS Lett. 370, 212-214.
    • (1995) FEBS Lett. , vol.370 , pp. 212-214
    • Cléry, C.1    Renault, F.2    Masson, P.3
  • 46
    • 0009744303 scopus 로고
    • Les hautes pressions: Outil d'investigation biochimique
    • Balny, C. & Masson, P. (1988) Les hautes pressions: outil d'investigation biochimique. Innov. Tech. Biol. Med. 9, 294-320.
    • (1988) Innov. Tech. Biol. Med. , vol.9 , pp. 294-320
    • Balny, C.1    Masson, P.2
  • 47
    • 0000530810 scopus 로고
    • High pressure kinetics in solution
    • Eckert, C.A. (1972) High pressure kinetics in solution. Annu. Rev. Phys. Chem. 23, 239-264.
    • (1972) Annu. Rev. Phys. Chem. , vol.23 , pp. 239-264
    • Eckert, C.A.1
  • 48
    • 33845184910 scopus 로고
    • Activation and reaction volumes in solution
    • Van Eldik, R., Asano, T. & Le Noble, W.J. (1989) Activation and reaction volumes in solution. Chem, Rev. 89, 549-688.
    • (1989) Chem. Rev. , vol.89 , pp. 549-688
    • Van Eldik, R.1    Asano, T.2    Le Noble, W.J.3
  • 49
    • 4243468938 scopus 로고    scopus 로고
    • The cation-π interaction
    • Ma, J.C. & Dougherty, D.A. (1997) The cation-π interaction. Chem. Rev. 97, 1303-1324.
    • (1997) Chem. Rev. , vol.97 , pp. 1303-1324
    • Ma, J.C.1    Dougherty, D.A.2
  • 50
    • 0009714969 scopus 로고
    • Pressure enhancement of charge-transfer complexing of 1-methyl-3-(carbomethoxy) pyridinium cation and 8-chlorotheophyllinate anion in aqueous solution
    • Williams, R.K. (1981) Pressure enhancement of charge-transfer complexing of 1-methyl-3-(carbomethoxy) pyridinium cation and 8-chlorotheophyllinate anion in aqueous solution. J. Phys. Chem. 85, 1795-1799.
    • (1981) J. Phys. Chem. , vol.85 , pp. 1795-1799
    • Williams, R.K.1
  • 51
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff, S.N. (1998) Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem. 51, 355-432.
    • (1998) Adv. Protein Chem. , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 52
    • 0032560503 scopus 로고    scopus 로고
    • In disperse solution 'osmotic stress' is a restricted case of preferential interactions
    • Timasheff, S.N. (1998) In disperse solution 'osmotic stress' is a restricted case of preferential interactions. Proc. Natl Acad. Sci. USA 95, 7363-7367.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7363-7367
    • Timasheff, S.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.