메뉴 건너뛰기




Volumn 139, Issue 6, 2006, Pages 1025-1033

Molten globule-like state of bovine carbonic anhydrase in the presence of acetonitrile

Author keywords

Acetonitrile; Carbonic anhydrase; Molten globule; Organic solvent; Thermal stability

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ACETONITRILE; BUFFER; CARBONATE DEHYDRATASE II; IODIDE ION; TRYPTOPHAN;

EID: 33746928416     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvj115     Document Type: Article
Times cited : (15)

References (33)
  • 1
    • 0026463503 scopus 로고
    • Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes
    • Hakansson, K., Carlsson, M., Svensson, L.A., and Lilijas, A. (1992) Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes. J. Mol. Biol. 227, 1192-1204
    • (1992) J. Mol. Biol. , vol.227 , pp. 1192-1204
    • Hakansson, K.1    Carlsson, M.2    Svensson, L.A.3    Lilijas, A.4
  • 2
    • 10044246302 scopus 로고    scopus 로고
    • Origin of mechanical strength of bovine carbonic anhydrase studied by molecular dynamics simulation
    • Ohta, S. Alam, M.T., Arakawa, H., and Ikai, A. (2004) Origin of mechanical strength of bovine carbonic anhydrase studied by molecular dynamics simulation. Biophys. J. 87, 4007-4020
    • (2004) Biophys. J. , vol.87 , pp. 4007-4020
    • Ohta, S.1    Alam, M.T.2    Arakawa, H.3    Ikai, A.4
  • 4
    • 3543137968 scopus 로고
    • Inherited variant of erythrocyte carbonic anhydrase in Micronesians from Guam and Saipan
    • Tashian, R.E., Plato, C.C., and Shows, T.B. (1963) Inherited variant of erythrocyte carbonic anhydrase in Micronesians from Guam and Saipan. Science 140, 53-54
    • (1963) Science , vol.140 , pp. 53-54
    • Tashian, R.E.1    Plato, C.C.2    Shows, T.B.3
  • 5
    • 0014180115 scopus 로고
    • Studies of the esterase activity and the anion inhibition of bovine zinc and cobalt carbonic anhydrases
    • Thorslund, A. and Lindskog, S. (1967) Studies of the esterase activity and the anion inhibition of bovine zinc and cobalt carbonic anhydrases. Eur. J. Biochem. 3, 117-123
    • (1967) Eur. J. Biochem. , vol.3 , pp. 117-123
    • Thorslund, A.1    Lindskog, S.2
  • 7
    • 0031104802 scopus 로고    scopus 로고
    • Why are enzymes less active in organic solvents than in water?
    • Klibanov, A.M. (1997) Why are enzymes less active in organic solvents than in water? Trends Biotechnol. 15, 97-101
    • (1997) Trends Biotechnol. , vol.15 , pp. 97-101
    • Klibanov, A.M.1
  • 8
    • 0034657542 scopus 로고    scopus 로고
    • Enhancement of catalytic efficiency of enzymes through exposure to anhydrous organic solvent at 70 degrees C. Three-dimensional structure of a treated serine proteinase at 2.2 Å resolution
    • Gupta, M.N., Tyagi, R., Sharma, S., Karthikeyan, S., and Singh, T.P. (2000) Enhancement of catalytic efficiency of enzymes through exposure to anhydrous organic solvent at 70 degrees C. Three-dimensional structure of a treated serine proteinase at 2.2 Å resolution. Proteins 39, 226-34
    • (2000) Proteins , vol.39 , pp. 226-234
    • Gupta, M.N.1    Tyagi, R.2    Sharma, S.3    Karthikeyan, S.4    Singh, T.P.5
  • 10
    • 0026701686 scopus 로고
    • Solid-state NMR assessment of enzyme active center structure under non-aqueous conditions
    • Burke, P.A., Griffin, R.G., and Klibanov, A.M. (1992) Solid-state NMR assessment of enzyme active center structure under non-aqueous conditions. J. Biol. Chem. 267, 20057-20064
    • (1992) J. Biol. Chem. , vol.267 , pp. 20057-20064
    • Burke, P.A.1    Griffin, R.G.2    Klibanov, A.M.3
  • 12
    • 4143127620 scopus 로고    scopus 로고
    • Hydration of enzyme in non-aqueous media is consistent with solvent dependence of its activity
    • Yang, L., Dordick, J.S., and Garde, S. (2004) Hydration of enzyme in non-aqueous media is consistent with solvent dependence of its activity. Biophys. J. 87, 812-821
    • (2004) Biophys. J. , vol.87 , pp. 812-821
    • Yang, L.1    Dordick, J.S.2    Garde, S.3
  • 14
    • 0028243728 scopus 로고
    • X-ray crystal structure of gamma-chymotrypsin in hexane
    • Yennawar, N.H., Yennawar, H.P., and Farber, G.K. (1994) X-ray crystal structure of gamma-chymotrypsin in hexane. Biochemistry 33, 7326-7336
    • (1994) Biochemistry , vol.33 , pp. 7326-7336
    • Yennawar, N.H.1    Yennawar, H.P.2    Farber, G.K.3
  • 16
    • 0030970824 scopus 로고    scopus 로고
    • The crystal structure of subtilisin Carlsberg in anhydrous dioxane and its comparison with those in water and acetonitrile
    • Schmitke, J.L., Stern, L.J., and Klibanov, A.M. (1997) The crystal structure of subtilisin Carlsberg in anhydrous dioxane and its comparison with those in water and acetonitrile. Proc. Natl. Acad. Sci. USA 94, 4250-4255
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4250-4255
    • Schmitke, J.L.1    Stern, L.J.2    Klibanov, A.M.3
  • 17
    • 0032573075 scopus 로고    scopus 로고
    • Comparison of x-ray crystal structures of an acyl-enzyme intermediate of subtilisin Carlsberg formed in anhydrous acetonitrile and in water
    • Schmitke, J.L., Stern, L.J., and Klibanov, A.M. (1998) Comparison of x-ray crystal structures of an acyl-enzyme intermediate of subtilisin Carlsberg formed in anhydrous acetonitrile and in water. Proc. Natl. Acad. Sci. USA 95, 12918-12923
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12918-12923
    • Schmitke, J.L.1    Stern, L.J.2    Klibanov, A.M.3
  • 18
    • 0032551728 scopus 로고    scopus 로고
    • Organic solvent binding to crystalline subtilisin1 in mostly aqueous media and in the neat solvents
    • Schmitke, J.L., Stern, L.J., and Klibanov, A.M. (1998) Organic solvent binding to crystalline subtilisin1 in mostly aqueous media and in the neat solvents. Biochem. Biophys. Res. Commun. 248, 273-277
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 273-277
    • Schmitke, J.L.1    Stern, L.J.2    Klibanov, A.M.3
  • 20
    • 0000341367 scopus 로고
    • Protein flexibility in aqueous and non-aqueous solutions
    • Hartsough, D.S. and Merz, K.M. (1992) Protein flexibility in aqueous and non-aqueous solutions. J. Am. Chem. Soc. 114, 10113-10116.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10113-10116
    • Hartsough, D.S.1    Merz, K.M.2
  • 21
    • 0001159492 scopus 로고
    • Protein dynamics, and salvation in aqueous, and nonaqueous environments
    • Hartsough, D.S. and Merz, K.M. (1993) Protein dynamics, and salvation in aqueous, and nonaqueous environments. J. Am. Chem. Soc. 115, 6529-6537
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 6529-6537
    • Hartsough, D.S.1    Merz, K.M.2
  • 22
    • 0000764219 scopus 로고
    • Solvent variation inverts substrate specificity of an enzyme
    • Wescott, C.R. and Klibanov, A.M. (1993) Solvent variation inverts substrate specificity of an enzyme. J. Am. Chem. Soc. 115, 1629-1631
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 1629-1631
    • Wescott, C.R.1    Klibanov, A.M.2
  • 23
    • 0028302684 scopus 로고
    • The solvent dependence of enzyme specificity
    • Wescott, C.R. and Klibanov, A.M. (1994) The solvent dependence of enzyme specificity. Biochim. Biophys. Acta 1206, 1-9
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 1-9
    • Wescott, C.R.1    Klibanov, A.M.2
  • 24
    • 0028855057 scopus 로고
    • Role of solvents in the control of enzyme selectivity in organic media
    • Carrea, G., Ottolina, G., and Riva, S. (1995) Role of solvents in the control of enzyme selectivity in organic media. Trends Biotechnol. 13, 63-70
    • (1995) Trends Biotechnol. , vol.13 , pp. 63-70
    • Carrea, G.1    Ottolina, G.2    Riva, S.3
  • 25
    • 0014011587 scopus 로고
    • Purification and properties of human erythrocyte carbonic anhydrases
    • Armstrong, J.M., Meyrs, D.V., Verpoorte, J.A., and Edsall, J.T. (1966) Purification and properties of human erythrocyte carbonic anhydrases. J. Biol. Chem. 241, 5137-5149
    • (1966) J. Biol. Chem. , vol.241 , pp. 5137-5149
    • Armstrong, J.M.1    Meyrs, D.V.2    Verpoorte, J.A.3    Edsall, J.T.4
  • 26
    • 0014062860 scopus 로고
    • The catalytic versatility of erythrocyte carbonic anhydrase. III. Kinetic studies of the enzyme-catalyzed hydrolysis of p-nitrophenyl acetate
    • Pocker Y. and Stone J. T. (1967) The catalytic versatility of erythrocyte carbonic anhydrase. III. Kinetic studies of the enzyme-catalyzed hydrolysis of p-nitrophenyl acetate. Biochemistry 6, 668-678
    • (1967) Biochemistry , vol.6 , pp. 668-678
    • Pocker, Y.1    Stone, J.T.2
  • 27
    • 0000750472 scopus 로고
    • Amino acid composition of various forms of bovine and human erythrocyte carbonic anhydrase
    • Nyman, P.O. and Lindskog, S. (1964) Amino acid composition of various forms of bovine and human erythrocyte carbonic anhydrase. Biochim. Biophys. Acta 85, 141-151
    • (1964) Biochim. Biophys. Acta , vol.85 , pp. 141-151
    • Nyman, P.O.1    Lindskog, S.2
  • 28
    • 0026530383 scopus 로고
    • Quantitative analysis of protein far UV circular dichroism spectra by neural networks
    • Bohm, G., Muhr, R., and Jaenicke, R. (1992) Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Eng. 5, 191-195
    • (1992) Protein Eng. , vol.5 , pp. 191-195
    • Bohm, G.1    Muhr, R.2    Jaenicke, R.3
  • 30
    • 0030005250 scopus 로고    scopus 로고
    • Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides
    • Wimley, W.C., Creamer, T.P., and White, S.H. (1996) Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides. Biochemistry 35, 5109-5124
    • (1996) Biochemistry , vol.35 , pp. 5109-5124
    • Wimley, W.C.1    Creamer, T.P.2    White, S.H.3
  • 31
    • 0030956720 scopus 로고    scopus 로고
    • Anionic phospholipids modulate peptide insertion into membranes
    • Liu, L.P. and Deber, C.M. (1997) Anionic phospholipids modulate peptide insertion into membranes. Biochemistry 36, 5476-5482
    • (1997) Biochemistry , vol.36 , pp. 5476-5482
    • Liu, L.P.1    Deber, C.M.2
  • 32
    • 0030772018 scopus 로고    scopus 로고
    • Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine
    • Briganti, F., Mangani, S., Orioli, P., Scozzafava, A., Vernaglione, G., and Supuran, C.T. (1997) Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine. Biochemistry 36, 10384-10392
    • (1997) Biochemistry , vol.36 , pp. 10384-10392
    • Briganti, F.1    Mangani, S.2    Orioli, P.3    Scozzafava, A.4    Vernaglione, G.5    Supuran, C.T.6
  • 33
    • 0015866154 scopus 로고
    • Environment and exposure to solvent of protein atoms. Lysozyme and insulin
    • Shrake, A. and Rupley, J.A. (1973) Environment and exposure to solvent of protein atoms. Lysozyme and insulin. J. Mol. Biol. 79, 351-371
    • (1973) J. Mol. Biol. , vol.79 , pp. 351-371
    • Shrake, A.1    Rupley, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.