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Volumn 270, Issue 24, 2003, Pages 4823-4834

Perturbation of folding and reassociation of lactate dehydrogenase by proline and trimethylamine oxide

Author keywords

Lactate dehydrogenase; Osmolytes; Proline; Renaturation; Trimethylamine oxide

Indexed keywords

AMINO ACID; LACTATE DEHYDROGENASE; PROLINE; TRIMETHYLAMINE OXIDE;

EID: 0346880116     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03881.x     Document Type: Article
Times cited : (24)

References (45)
  • 1
    • 0018641198 scopus 로고
    • Counteraction of urea destabilization of protein structure by methylamine osmoregulatory compounds of elasmobranch fishes
    • Yancey, P.H. & Somero, G.N. (1979) Counteraction of urea destabilization of protein structure by methylamine osmoregulatory compounds of elasmobranch fishes. Biochem. J. 183, 317-323.
    • (1979) Biochem. J. , vol.183 , pp. 317-323
    • Yancey, P.H.1    Somero, G.N.2
  • 2
    • 0028787409 scopus 로고
    • Effects of a naturally occurring compatible osmolyte on the internal dynamics of ribonuclease A
    • Wang, A., Robertson, A.D. & Bolen, D.W. (1995) Effects of a naturally occurring compatible osmolyte on the internal dynamics of ribonuclease A. Biochemistry 34, 15096-15104.
    • (1995) Biochemistry , vol.34 , pp. 15096-15104
    • Wang, A.1    Robertson, A.D.2    Bolen, D.W.3
  • 3
    • 0031967834 scopus 로고    scopus 로고
    • Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: A test of the counteraction hypothesis
    • Baskakov, I., Wang, A. & Bolen, D.W. (1998) Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: a test of the counteraction hypothesis. Biophys. J. 74, 2666-2673.
    • (1998) Biophys. J. , vol.74 , pp. 2666-2673
    • Baskakov, I.1    Wang, A.2    Bolen, D.W.3
  • 4
    • 0028150954 scopus 로고
    • Why do some organisms use a urea-methylamine mixture as osmolyte? Thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein
    • Lin, T.Y. & Timasheff, S.N. (1994) Why do some organisms use a urea-methylamine mixture as osmolyte? Thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein. Biochemistry 33, 12695-12701.
    • (1994) Biochemistry , vol.33 , pp. 12695-12701
    • Lin, T.Y.1    Timasheff, S.N.2
  • 5
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: Natural selection of a thermodynamic force in protein folding
    • Bolen, D.W. & Baskakov, I.V. (2001) The osmophobic effect: natural selection of a thermodynamic force in protein folding. J. Mol. Biol. 310, 955-963.
    • (2001) J. Mol. Biol. , vol.310 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2
  • 6
    • 0030154620 scopus 로고    scopus 로고
    • Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein
    • Brown, C.R., Hong-Brown, L.Q., Biwersi, J., Verkman, A.S. & Welch, W.J. (1996) Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein. Cell Stress Chaperones 1, 117-125.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 117-125
    • Brown, C.R.1    Hong-Brown, L.Q.2    Biwersi, J.3    Verkman, A.S.4    Welch, W.J.5
  • 7
    • 0032039542 scopus 로고    scopus 로고
    • Multiple effects of trehalose on protein folding in vitro and in vivo
    • Singer, M.A. & Lindquist, S. (1998) Multiple effects of trehalose on protein folding in vitro and in vivo. Mol. Cell 1, 639-648.
    • (1998) Mol. Cell , vol.1 , pp. 639-648
    • Singer, M.A.1    Lindquist, S.2
  • 8
    • 0032213339 scopus 로고    scopus 로고
    • Thermotolerance in Saccharomyces cerevisiae: The Yin and Yang of trehalose
    • Singer, M.A. & Lindquist, S. (1998) Thermotolerance in Saccharomyces cerevisiae: the Yin and Yang of trehalose. Trends Biotechnol. 16, 460-468.
    • (1998) Trends Biotechnol. , vol.16 , pp. 460-468
    • Singer, M.A.1    Lindquist, S.2
  • 9
    • 0030154323 scopus 로고    scopus 로고
    • Influence of molecular and chemical chaperones on protein folding
    • Welch, W.J. & Brown, C.R. (1996) Influence of molecular and chemical chaperones on protein folding. Cell Stress Chaperones 1, 109-115.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 109-115
    • Welch, W.J.1    Brown, C.R.2
  • 10
    • 0029832863 scopus 로고    scopus 로고
    • Chemical chaperones interfere with the formation of scrapie prion protein
    • Tatzelt, J., Prusiner, S.B. & Welch, W.J. (1996) Chemical chaperones interfere with the formation of scrapie prion protein. EMBO J. 15, 6363-6373.
    • (1996) EMBO J. , vol.15 , pp. 6363-6373
    • Tatzelt, J.1    Prusiner, S.B.2    Welch, W.J.3
  • 12
    • 0017178879 scopus 로고
    • The refolding of lactate dehydrogenase subunits and their assembly to the functional tetramer
    • Tenenbaum-Bayer, H. & Levitzki, A. (1976) The refolding of lactate dehydrogenase subunits and their assembly to the functional tetramer. Biochim. Biophys. Acta 445, 261-279.
    • (1976) Biochim. Biophys. Acta , vol.445 , pp. 261-279
    • Tenenbaum-Bayer, H.1    Levitzki, A.2
  • 13
    • 0001224536 scopus 로고
    • Intermediates in the folding pathway of octopine dehydrogenase from pectin jacobaeus
    • Teschner, W., Rudolph, R. & Garel, J.-R. (1987) Intermediates in the folding pathway of octopine dehydrogenase from pectin jacobaeus. Biochemistry 26, 2791-2796.
    • (1987) Biochemistry , vol.26 , pp. 2791-2796
    • Teschner, W.1    Rudolph, R.2    Garel, J.-R.3
  • 14
    • 0036152775 scopus 로고    scopus 로고
    • Effect of osmolytes as folding aids on creatine kinase refolding pathway
    • Ou, W.B., Park, Y.D. & Zhou, H.M. (2002) Effect of osmolytes as folding aids on creatine kinase refolding pathway. Int. J. Biochem. Cell Biol. 34, 136-147.
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 136-147
    • Ou, W.B.1    Park, Y.D.2    Zhou, H.M.3
  • 15
    • 0034581324 scopus 로고    scopus 로고
    • Folding and association of oligomeric and multimeric proteins
    • Jaenicke, R. & Lilie, H. (2000) Folding and association of oligomeric and multimeric proteins. Adv. Protein Chem. 53, 329-401.
    • (2000) Adv. Protein Chem. , vol.53 , pp. 329-401
    • Jaenicke, R.1    Lilie, H.2
  • 16
    • 0031737071 scopus 로고    scopus 로고
    • The role of proline in the prevention of aggregation during protein folding in vitro
    • Kumar, T.K., Samuel, D., Jayaraman, G., Srimathi, T. & Yu, C. (1998) The role of proline in the prevention of aggregation during protein folding in vitro. Biochem. Mol. Biol. Int. 46, 509-517.
    • (1998) Biochem. Mol. Biol. Int. , vol.46 , pp. 509-517
    • Kumar, T.K.1    Samuel, D.2    Jayaraman, G.3    Srimathi, T.4    Yu, C.5
  • 17
    • 0000532545 scopus 로고
    • The comparative enzymology of lactate dehydrogenases I. Properties of the crystalline beef and chicken enzymes
    • Pesce, A., McKay, R.H., Stolzenbach, F., Cahn, R.D. & Kaplan, N.O. (1964) The comparative enzymology of lactate dehydrogenases I. Properties of the crystalline beef and chicken enzymes. J. Biol. Chem. 239, 1753-1761.
    • (1964) J. Biol. Chem. , vol.239 , pp. 1753-1761
    • Pesce, A.1    McKay, R.H.2    Stolzenbach, F.3    Cahn, R.D.4    Kaplan, N.O.5
  • 18
    • 0019619407 scopus 로고
    • Reassociation of lactic dehydrogenase from pig heart studied by cross-linking with glutaraldehyde
    • Bernhardt, G., Rudolph, R. & Jaenicke, R. (1981) Reassociation of lactic dehydrogenase from pig heart studied by cross-linking with glutaraldehyde. Z. Naturforsch. [C] 36, 772-777.
    • (1981) Z. Naturforsch. [C] , vol.36 , pp. 772-777
    • Bernhardt, G.1    Rudolph, R.2    Jaenicke, R.3
  • 19
    • 0014016769 scopus 로고
    • Developmental redistributions of porcine lactate dehydrogenase
    • Fieldhouse, B. & Masters, C.J. (1966) Developmental redistributions of porcine lactate dehydrogenase. Biochim. Biophys. Acta 118, 538-548.
    • (1966) Biochim. Biophys. Acta , vol.118 , pp. 538-548
    • Fieldhouse, B.1    Masters, C.J.2
  • 21
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. & Peitsch, M.C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 22
    • 0036470051 scopus 로고    scopus 로고
    • Protein explorer: Easy yet powerful macromolecular visualization
    • Martz, E. (2002) Protein explorer: easy yet powerful macromolecular visualization. Trends Biochem. Sci. 27, 107-109.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 107-109
    • Martz, E.1
  • 23
    • 0032169688 scopus 로고    scopus 로고
    • PQS: A protein quaternary structure file server
    • Henrick, K. & Thornton, J.M. (1998) PQS: a protein quaternary structure file server. Trends Biochem. Sci. 23, 358-361.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 358-361
    • Henrick, K.1    Thornton, J.M.2
  • 24
    • 0017744370 scopus 로고
    • Mechanism of refolding and reactivation of lactic dehydrogenase from pig heart after dissociation in various solvent media
    • Rudolph, R., Heider, I., Westhof, E. & Jaenicke, R. (1977) Mechanism of refolding and reactivation of lactic dehydrogenase from pig heart after dissociation in various solvent media. Biochemistry 16, 3384-3390.
    • (1977) Biochemistry , vol.16 , pp. 3384-3390
    • Rudolph, R.1    Heider, I.2    Westhof, E.3    Jaenicke, R.4
  • 25
    • 0017888990 scopus 로고
    • Unusual solution properties of proline and its interaction with proteins
    • Schobert, B. & Tschesche, H. (1978) Unusual solution properties of proline and its interaction with proteins. Biochim. Biophys. Acta 541, 270-277.
    • (1978) Biochim. Biophys. Acta , vol.541 , pp. 270-277
    • Schobert, B.1    Tschesche, H.2
  • 26
    • 0017390347 scopus 로고
    • The anomalous colligative properties of proline
    • Schobert, B. (1977) The anomalous colligative properties of proline. Naturwissenschaften 64, 386.
    • (1977) Naturwissenschaften , vol.64 , pp. 386
    • Schobert, B.1
  • 27
    • 0023506457 scopus 로고
    • Folding and association of proteins
    • Jaenicke, R. (1987) Folding and association of proteins. Prog. Biophys. Mol. Biol. 49, 117-237.
    • (1987) Prog. Biophys. Mol. Biol. , vol.49 , pp. 117-237
    • Jaenicke, R.1
  • 29
    • 0014933421 scopus 로고
    • Physiological concentrations of lactate dehydrogenases and substrate inhibition
    • Everse, J., Berger, R.L. & Kaplan, N.O. (1970) Physiological concentrations of lactate dehydrogenases and substrate inhibition. Science 168, 1236-1238.
    • (1970) Science , vol.168 , pp. 1236-1238
    • Everse, J.1    Berger, R.L.2    Kaplan, N.O.3
  • 31
    • 0020336190 scopus 로고
    • Living with water stress: Evolution of osmolyte systems
    • Yancey, P.H., Clark, M.E., Hand, S.C., Bowlus, R.D. & Somero, G.N. (1982) Living with water stress: evolution of osmolyte systems. Science 217, 1214-1222.
    • (1982) Science , vol.217 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, S.C.3    Bowlus, R.D.4    Somero, G.N.5
  • 32
    • 0033011365 scopus 로고    scopus 로고
    • High contents of trimethylamine oxide correlating with depth in deep-sea teleost fishes, skates, and decapod crustations
    • Kelly, R.H. & Yancey, P.H. (1999) High contents of trimethylamine oxide correlating with depth in deep-sea teleost fishes, skates, and decapod crustations. Biol. Bull. 196, 18-25.
    • (1999) Biol. Bull. , vol.196 , pp. 18-25
    • Kelly, R.H.1    Yancey, P.H.2
  • 33
    • 0036848921 scopus 로고    scopus 로고
    • Unusual organic osmolytes in deep-sea animals: Adaptations to hydrostatic pressure and other perturbants
    • Yancey, P.H., Blake, W.R. & Conley, J. (2002) Unusual organic osmolytes in deep-sea animals: adaptations to hydrostatic pressure and other perturbants. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 133, 667-676.
    • (2002) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.133 , pp. 667-676
    • Yancey, P.H.1    Blake, W.R.2    Conley, J.3
  • 34
    • 0035865755 scopus 로고    scopus 로고
    • Trimethylamine oxide counteracts effects of hydrostatic pressure on proteins of deep-sea teleosts
    • Yancey, P.H., Fyfe-Johnson, A.L., Kelly, R.H., Walker, V.P. & Aunon, M.T. (2001) Trimethylamine oxide counteracts effects of hydrostatic pressure on proteins of deep-sea teleosts. J. Exp. Zool. 289, 172-176.
    • (2001) J. Exp. Zool. , vol.289 , pp. 172-176
    • Yancey, P.H.1    Fyfe-Johnson, A.L.2    Kelly, R.H.3    Walker, V.P.4    Aunon, M.T.5
  • 35
    • 0035955743 scopus 로고    scopus 로고
    • Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses
    • Diamant, S., Eliahu, N., Rosenthal, D. & Goloubinoff, P. (2001) Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses. J. Biol. Chem. 276, 39586-39591.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39586-39591
    • Diamant, S.1    Eliahu, N.2    Rosenthal, D.3    Goloubinoff, P.4
  • 36
    • 0019616577 scopus 로고
    • Analysis of the reconstitution of oligomeric enzymes by cross-linking with glutaraldehyde: Kinetics of reassociation of lactic dehydrogenase
    • Hermann, R., Jaenicke, R. & Rudolph, R. (1981) Analysis of the reconstitution of oligomeric enzymes by cross-linking with glutaraldehyde: kinetics of reassociation of lactic dehydrogenase. Biochemistry 20, 5195-5201.
    • (1981) Biochemistry , vol.20 , pp. 5195-5201
    • Hermann, R.1    Jaenicke, R.2    Rudolph, R.3
  • 37
    • 76549146190 scopus 로고
    • Lactate dehydrogenases - Structure and function
    • Kaplan, N.O. (1964) Lactate dehydrogenases - structure and function. Brookhaven Symp. Biol. 17, 131-153.
    • (1964) Brookhaven Symp. Biol. , vol.17 , pp. 131-153
    • Kaplan, N.O.1
  • 38
    • 0032483027 scopus 로고    scopus 로고
    • Osmolyte-driven contraction of a random coil protein
    • Qu, Y., Bolen, C.L. & Bolen, D.W. (1998) Osmolyte-driven contraction of a random coil protein. Proc. Natl Acad. Sci. USA 95, 9268-9273.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9268-9273
    • Qu, Y.1    Bolen, C.L.2    Bolen, D.W.3
  • 40
    • 0017595429 scopus 로고
    • Modification of pig heart lactate dehydrogenase with methyl methanethiosulphonate to produce an enzyme with altered catalytic activity
    • Bloxham, D.P. & Wilton, D.C. (1977) Modification of pig heart lactate dehydrogenase with methyl methanethiosulphonate to produce an enzyme with altered catalytic activity. Biochem. J. 161, 643-651.
    • (1977) Biochem. J. , vol.161 , pp. 643-651
    • Bloxham, D.P.1    Wilton, D.C.2
  • 41
    • 0023051846 scopus 로고
    • Conformational drift of dissociated lactate dehydrogenases
    • King, L. & Weber, G. (1986) Conformational drift of dissociated lactate dehydrogenases. Biochemistry 25, 3632-3637.
    • (1986) Biochemistry , vol.25 , pp. 3632-3637
    • King, L.1    Weber, G.2
  • 42
    • 0028360784 scopus 로고
    • Proline-protein interactions: Protection of structural and functional integrity of M4 lactate dehydrogenase
    • Rajendrakumar, C.S., Reddy, B.V. & Reddy, A.R. (1994) Proline-protein interactions: protection of structural and functional integrity of M4 lactate dehydrogenase. Biochem. Biophys. Res. Commun. 201, 957-963.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 957-963
    • Rajendrakumar, C.S.1    Reddy, B.V.2    Reddy, A.R.3
  • 43
    • 0002733477 scopus 로고    scopus 로고
    • Stabilization of protein structure by osmolytes
    • Creighton, T.E., ed., IRL Press, Oxford
    • Timasheff, S.N. & Arakawa, T. (1997) Stabilization of protein structure by osmolytes. In Protein Structure: a Practical Approach (Creighton, T.E., ed.), pp. 344-364. IRL Press, Oxford.
    • (1997) Protein Structure: A Practical Approach , pp. 344-364
    • Timasheff, S.N.1    Arakawa, T.2
  • 44
    • 0029812281 scopus 로고    scopus 로고
    • Effect of proline on lactate dehydrogenase activity: Testing the generality and scope of the compatibility paradigm
    • Wang, A. & Bolen, D.W. (1996) Effect of proline on lactate dehydrogenase activity: testing the generality and scope of the compatibility paradigm. Biophys. J. 71, 2117-2122.
    • (1996) Biophys. J. , vol.71 , pp. 2117-2122
    • Wang, A.1    Bolen, D.W.2
  • 45
    • 0031965750 scopus 로고    scopus 로고
    • Time-dependent effects of trimethylamine-N-oxide/urea on lactate dehydrogenase activity: An unexplored dimension of the adaptation paradigm
    • Baskakov, I. & Bolen, D.W. (1998) Time-dependent effects of trimethylamine-N-oxide/urea on lactate dehydrogenase activity: an unexplored dimension of the adaptation paradigm. Biophys. J. 74, 2658-2665.
    • (1998) Biophys. J. , vol.74 , pp. 2658-2665
    • Baskakov, I.1    Bolen, D.W.2


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