메뉴 건너뛰기




Volumn 40, Issue 2, 2000, Pages 207-217

Electrostatics of mesophilic and psychrophilic trypsin isoenzymes: Qualitative evaluation of electrostatic differences at the substrate binding site

Author keywords

Cold adapted trypsins; Poisson Boltzmann; Potential; Specificity pocket; Substrate binding

Indexed keywords

ISOENZYME; TRYPSIN;

EID: 0034257240     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(20000801)40:2<207::AID-PROT40>3.0.CO;2-U     Document Type: Article
Times cited : (39)

References (42)
  • 1
    • 0030699980 scopus 로고    scopus 로고
    • Psychrophilic enzymes: A thermodynamic challenge
    • Gerday C, Aittaleb M, Arpigny JL, et al. Psychrophilic enzymes: a thermodynamic challenge. Biochem Biophys Acta 1997;1342:119-131.
    • (1997) Biochem Biophys Acta , vol.1342 , pp. 119-131
    • Gerday, C.1    Aittaleb, M.2    Arpigny, J.L.3
  • 4
    • 0029851195 scopus 로고    scopus 로고
    • Temperature and pH sensitivity of trypsins from atlantic salmon (Salmo salar) in comparison with bovine and porcine trypsin
    • Outzen H, Berglund GI, Smalås AO, Willassen NP. Temperature and pH sensitivity of trypsins from atlantic salmon (Salmo salar) in comparison with bovine and porcine trypsin. Comp Biochem Biophys 1996;115B:33-45.
    • (1996) Comp Biochem Biophys , vol.115 B , pp. 33-45
    • Outzen, H.1    Berglund, G.I.2    Smalås, A.O.3    Willassen, N.P.4
  • 5
    • 0024638262 scopus 로고
    • Purification and characterization of trypsin from the poikilotherm Gadus morhua
    • Asgeirsson B, Fox JW, Bjarnason JB. Purification and characterization of trypsin from the poikilotherm Gadus morhua. Eur J Biochem 1989;180:85-94.
    • (1989) Eur J Biochem , vol.180 , pp. 85-94
    • Asgeirsson, B.1    Fox, J.W.2    Bjarnason, J.B.3
  • 6
    • 0000618105 scopus 로고
    • Trypsin from the antarctic fish (Paranotothenia magellanica forster) as compared with trout (Salmo gairdneri) trypsin
    • Genicot S, Feller G, Gerday C. Trypsin from the antarctic fish (Paranotothenia magellanica forster) as compared with trout (Salmo gairdneri) trypsin. Comp Biochem Physiol 1988;90B:601-609.
    • (1988) Comp Biochem Physiol , vol.90 B , pp. 601-609
    • Genicot, S.1    Feller, G.2    Gerday, C.3
  • 7
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I, Berger A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 1967;27:157-162.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 8
    • 0033612211 scopus 로고    scopus 로고
    • Interscaffolding additivity: Binding of P1 variants of bovine pancreatic trypsin inhibitor to four serine proteinases
    • Krowarsch D, Dadlez M, Buczek O, Krokoszynska I, Smalås AO, Otlewski J. Interscaffolding additivity: binding of P1 variants of bovine pancreatic trypsin inhibitor to four serine proteinases. J Mol Biol 1999;289:175-186.
    • (1999) J Mol Biol , vol.289 , pp. 175-186
    • Krowarsch, D.1    Dadlez, M.2    Buczek, O.3    Krokoszynska, I.4    Smalås, A.O.5    Otlewski, J.6
  • 9
    • 0031698348 scopus 로고    scopus 로고
    • The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor
    • Holland R, Leiros I, Willassen NP, Berglund GI, Smalås AO. The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor. Eur J Biochem 1998;256:317-324.
    • (1998) Eur J Biochem , vol.256 , pp. 317-324
    • Holland, R.1    Leiros, I.2    Willassen, N.P.3    Berglund, G.I.4    Smalås, A.O.5
  • 11
    • 0344549848 scopus 로고    scopus 로고
    • Residue determinants and sequence analysis of cold-adapted trypsins
    • Leiros H-KS, Willassen NP, Smalås AO. Residue determinants and sequence analysis of cold-adapted trypsins. Extremophilies 1999;3:205-219.
    • (1999) Extremophilies , vol.3 , pp. 205-219
    • Leiros, H.-K.1    Willassen, N.P.2    Smalås, A.O.3
  • 12
    • 0005492283 scopus 로고    scopus 로고
    • Structural comparison of psychrophilic and mesophilic trypsins: Elucidating the molecular basis of cold-adaptation
    • Leiros H-KS, Willassen NP, Smalås AO. Structural comparison of psychrophilic and mesophilic trypsins: elucidating the molecular basis of cold-adaptation. Eur J Biochem 2000;267:1039-1049.
    • (2000) Eur J Biochem , vol.267 , pp. 1039-1049
    • Leiros, H.-K.1    Willassen, N.P.2    Smalås, A.O.3
  • 13
    • 0028033122 scopus 로고
    • Cold adaption of enzymes: Structural comparison between salmon and bovine trypsins
    • Smalås AO, Heimstad ES, Hordvik A, Willassen NP, Male R. Cold adaption of enzymes: structural comparison between salmon and bovine trypsins. Proteins 1994;20:149-166.
    • (1994) Proteins , vol.20 , pp. 149-166
    • Smalås, A.O.1    Heimstad, E.S.2    Hordvik, A.3    Willassen, N.P.4    Male, R.5
  • 15
    • 0025283002 scopus 로고
    • Electrostatic interactions in macromolecules: Theory and applications
    • Sharp KA, Honig B. Electrostatic interactions in macromolecules: theory and applications. Annu Rev Biophys Biophys Chem 1990; 19:301-332.
    • (1990) Annu Rev Biophys Biophys Chem , vol.19 , pp. 301-332
    • Sharp, K.A.1    Honig, B.2
  • 16
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • Richards FM. Areas, volumes, packing and protein structure. Annu Rev Biophys Bioeng 1977;6:151-176.
    • (1977) Annu Rev Biophys Bioeng , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 17
    • 0021813940 scopus 로고
    • On the calculation of electrostatic interactions in proteins
    • Gilson MK, Rashin A, Fine R, Honig B. On the calculation of electrostatic interactions in proteins. J Mol Biol 1985;184:503-516.
    • (1985) J Mol Biol , vol.184 , pp. 503-516
    • Gilson, M.K.1    Rashin, A.2    Fine, R.3    Honig, B.4
  • 18
    • 0023779259 scopus 로고
    • Calculation of the total electrostatic energy of a macromolecular system: Solvation energy, binding energies, and conformational analysis
    • Gilson MK, Honig B. Calculation of the total electrostatic energy of a macromolecular system: solvation energy, binding energies, and conformational analysis. Proteins 1988;4:7-18.
    • (1988) Proteins , vol.4 , pp. 7-18
    • Gilson, M.K.1    Honig, B.2
  • 19
    • 0027159949 scopus 로고
    • The molecular surface package
    • Connolly ML. The molecular surface package. J Mol Graphics 1993;11:139-141.
    • (1993) J Mol Graphics , vol.11 , pp. 139-141
    • Connolly, M.L.1
  • 20
    • 0021757436 scopus 로고
    • A new force field for molecular mechanical simulation of nucleic acids and proteins
    • Weiner SJ, Kollman PA, Case DA, et al. A new force field for molecular mechanical simulation of nucleic acids and proteins. J Am Chem Soc 1984;106:765-783.
    • (1984) J Am Chem Soc , vol.106 , pp. 765-783
    • Weiner, S.J.1    Kollman, P.A.2    Case, D.A.3
  • 21
    • 0017411710 scopus 로고
    • The protein data bank: A computer-based archival file for macromolecular structures
    • Bernstein FC, Koetzle TF, Williams GJB, et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. J Mol Biol 1977;112:535-542.
    • (1977) J Mol Biol , vol.112 , pp. 535-542
    • Bernstein, F.C.1    Koetzle, T.F.2    Williams, G.J.B.3
  • 22
    • 36749119973 scopus 로고
    • Deformable stochastic boundaries in molecular dynamics
    • Brooks CL, Karplus M. Deformable stochastic boundaries in molecular dynamics. J Chem Phys 1983;79:6312-6325.
    • (1983) J Chem Phys , vol.79 , pp. 6312-6325
    • Brooks, C.L.1    Karplus, M.2
  • 23
    • 0027081912 scopus 로고
    • SQUID: A program for the analysis and display of data from crystallography and molecular dynamics
    • Oldfield TJ. SQUID: a program for the analysis and display of data from crystallography and molecular dynamics. J Mol Graphics 1992;10:247-252.
    • (1992) J Mol Graphics , vol.10 , pp. 247-252
    • Oldfield, T.J.1
  • 24
    • 0026319199 scopus 로고
    • Protein folding and association: Insight from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp K, Honig B. Protein folding and association: insight from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct Funct Genet 1991;11:281-296.
    • (1991) Proteins Struct Funct Genet , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou J-Y, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr 1991;A47:110-119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 0032167924 scopus 로고    scopus 로고
    • Structure of a non-psychrophilic trypsin from a cold-adapted fish species
    • Schrøder H-K, Willassen NP, Smalås AO. Structure of a non-psychrophilic trypsin from a cold-adapted fish species. Acta Crystallogr 1998;D54:780-798.
    • (1998) Acta Crystallogr , vol.D54 , pp. 780-798
    • Schrøder, H.-K.1    Willassen, N.P.2    Smalås, A.O.3
  • 27
    • 0026046827 scopus 로고
    • 1.59 Å structure of trypsin at 120 K: Comparison of low temperature and room temperature structures
    • Earnest T, Fauman E, Craik CS, Stroud R. 1.59 Å structure of trypsin at 120 K: comparison of low temperature and room temperature structures. Proteins 1991;10:171-181.
    • (1991) Proteins , vol.10 , pp. 171-181
    • Earnest, T.1    Fauman, E.2    Craik, C.S.3    Stroud, R.4
  • 28
    • 0027516857 scopus 로고
    • Refined 1.6 Å resolution crystal structure of the complex formed between porcine β-trypsin and MCTI-A, a trypsin inhibitor of the squash family: Detailed comparison with bovine β-trypsin and its complex
    • Huang Q, Liu S, Tang Y. Refined 1.6 Å resolution crystal structure of the complex formed between porcine β-trypsin and MCTI-A, a trypsin inhibitor of the squash family: detailed comparison with bovine β-trypsin and its complex. J Mol Biol 1993;229:1022-1036.
    • (1993) J Mol Biol , vol.229 , pp. 1022-1036
    • Huang, Q.1    Liu, S.2    Tang, Y.3
  • 29
    • 84977303841 scopus 로고
    • The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors
    • Marquart M, Walter J, Deisenhofer J, Bode W, Huber R. The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors. Acta Crystallogr 1983;B39:480-490.
    • (1983) Acta Crystallogr , vol.B39 , pp. 480-490
    • Marquart, M.1    Walter, J.2    Deisenhofer, J.3    Bode, W.4    Huber, R.5
  • 30
    • 0022964504 scopus 로고
    • Focusing of electric fields in the active site of Cu-Zn superoxid dismutase: Effects of ionic strenght and amino-acid modification
    • Klapper I, Hagstrom R, Fine R, Sharp K, Honig B. Focusing of electric fields in the active site of Cu-Zn superoxid dismutase: effects of ionic strenght and amino-acid modification. Proteins 1986;1:47-59.
    • (1986) Proteins , vol.1 , pp. 47-59
    • Klapper, I.1    Hagstrom, R.2    Fine, R.3    Sharp, K.4    Honig, B.5
  • 31
    • 0023364022 scopus 로고
    • Computer simulations of diffusion of a substrate to an active site of an enzyme
    • Sharp K, Fine R, Honig B. Computer simulations of diffusion of a substrate to an active site of an enzyme. Science 1987;236:1460-1463.
    • (1987) Science , vol.236 , pp. 1460-1463
    • Sharp, K.1    Fine, R.2    Honig, B.3
  • 32
    • 0022368152 scopus 로고
    • Electrostatic field of the large fragment of Escherichia coli DNA polymerase I
    • Warwicker J, Ollis D, Richard FM, Steitz TA. Electrostatic field of the large fragment of Escherichia coli DNA polymerase I. J Mol Biol 1985;186:645-649.
    • (1985) J Mol Biol , vol.186 , pp. 645-649
    • Warwicker, J.1    Ollis, D.2    Richard, F.M.3    Steitz, T.A.4
  • 33
    • 0023280069 scopus 로고
    • Calculation of electrostatic potentials in an enzyme active site
    • Gilson MK, Honig B. Calculation of electrostatic potentials in an enzyme active site. Nature 1987;330:84-86.
    • (1987) Nature , vol.330 , pp. 84-86
    • Gilson, M.K.1    Honig, B.2
  • 34
    • 0028173135 scopus 로고
    • Calculation of electrostatic effects at the amino terminus of an alpha helix
    • Sitkoff D, Lockhart DJ, Sharp KA, Honig B. Calculation of electrostatic effects at the amino terminus of an alpha helix. Biophys J 1994;67:2251-2260.
    • (1994) Biophys J , vol.67 , pp. 2251-2260
    • Sitkoff, D.1    Lockhart, D.J.2    Sharp, K.A.3    Honig, B.4
  • 37
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B, Richards FM. The interpretation of protein structures: estimation of static accessibility. J Mol Biol 1971;55:379-400.
    • (1971) J Mol Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 38
    • 0029832603 scopus 로고    scopus 로고
    • Trypsin: A case study in the structural determinants of enzyme specificity
    • Hedstrom L. Trypsin: a case study in the structural determinants of enzyme specificity. Biol Chem 1996;377:465-470.
    • (1996) Biol Chem , vol.377 , pp. 465-470
    • Hedstrom, L.1
  • 39
    • 0027965324 scopus 로고
    • Converting trypsin to chymotrypsin: Ground state binding does not determine substrate specificity
    • Hedstrom L, Farr-Jones S, Kettner CA, Rutter WJ. Converting trypsin to chymotrypsin: ground state binding does not determine substrate specificity. Biochemistry 1994;33:8764-8769.
    • (1994) Biochemistry , vol.33 , pp. 8764-8769
    • Hedstrom, L.1    Farr-Jones, S.2    Kettner, C.A.3    Rutter, W.J.4
  • 40
    • 0026520387 scopus 로고
    • Converting trypsin to chymotrypsin: The role of surface loops
    • Hedstrom L, Szilagyi L, Rutter WJ. Converting trypsin to chymotrypsin: the role of surface loops. Science 1992;255:1249-1253.
    • (1992) Science , vol.255 , pp. 1249-1253
    • Hedstrom, L.1    Szilagyi, L.2    Rutter, W.J.3
  • 41
    • 0031813817 scopus 로고    scopus 로고
    • Converting trypsin to elastase: Substitution of the S1 site and adjacent loops reconstitutes esterase specificity but not amidase activity
    • Hung SH, Hedstrom L. Converting trypsin to elastase: substitution of the S1 site and adjacent loops reconstitutes esterase specificity but not amidase activity. Protein Eng 1998;11:669-673.
    • (1998) Protein Eng , vol.11 , pp. 669-673
    • Hung, S.H.1    Hedstrom, L.2
  • 42
    • 0032577184 scopus 로고    scopus 로고
    • How the substitution of K188 of trypsin binding site by aromatic amino acids can influence the processing of beta-casein
    • Chobert JM, Briand L, Tran V, Haertle T. How the substitution of K188 of trypsin binding site by aromatic amino acids can influence the processing of beta-casein. Biochem Biophys Res Commun 1998;246:847-858.
    • (1998) Biochem Biophys Res Commun , vol.246 , pp. 847-858
    • Chobert, J.M.1    Briand, L.2    Tran, V.3    Haertle, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.