메뉴 건너뛰기




Volumn 23, Issue 1, 2007, Pages 155-161

Stabilities and conformational transitions of various proteases in the presence of an organic solvent

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; CONFORMATIONS; ENZYME KINETICS; METHANOL; ORGANIC SOLVENTS; STABILITY;

EID: 33847155508     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp060252p     Document Type: Conference Paper
Times cited : (34)

References (35)
  • 1
    • 0035843122 scopus 로고    scopus 로고
    • Enzymes for chemical synthesis
    • Koeller, K. M.; Wong, C. H. Enzymes for chemical synthesis. Nature 2001, 409, 232-240.
    • (2001) Nature , vol.409 , pp. 232-240
    • Koeller, K.M.1    Wong, C.H.2
  • 3
    • 0035108407 scopus 로고    scopus 로고
    • Enzymes which are stable in the presence of organic solvents
    • Ogino, H.; Ishikawa, H. Enzymes which are stable in the presence of organic solvents. J. Biosci. Bioeng. 2001, 91, 109-116.
    • (2001) J. Biosci. Bioeng , vol.91 , pp. 109-116
    • Ogino, H.1    Ishikawa, H.2
  • 4
    • 0021764054 scopus 로고
    • Conformational studies on the inactivation of glyceraldehyde-3-phosphate dehydrogenase from the facultative thermophile Bacillus coagulons KU
    • McLinden, J. H.; Wong, K.-P.; Murdock, A. L.; Amelunxen, R. E. Conformational studies on the inactivation of glyceraldehyde-3-phosphate dehydrogenase from the facultative thermophile Bacillus coagulons KU. Arch. Biochem. Biophys. 1984, 233, 299-309.
    • (1984) Arch. Biochem. Biophys , vol.233 , pp. 299-309
    • McLinden, J.H.1    Wong, K.-P.2    Murdock, A.L.3    Amelunxen, R.E.4
  • 5
    • 0023118118 scopus 로고
    • Characterization of the unfolding of ribonuclease A in aqueous methanol solvents
    • Fink, A. L.; Painter, B. Characterization of the unfolding of ribonuclease A in aqueous methanol solvents. Biochemistry 1987, 26, 1665-1671.
    • (1987) Biochemistry , vol.26 , pp. 1665-1671
    • Fink, A.L.1    Painter, B.2
  • 6
    • 0026598584 scopus 로고
    • The thermal denaturation of ribonuclease A in aqueous-methanol solvents
    • Lustig, B.; Fink, A. L. The thermal denaturation of ribonuclease A in aqueous-methanol solvents. Biochim. Biophys. Acta 1992, 1119, 205-210.
    • (1992) Biochim. Biophys. Acta , vol.1119 , pp. 205-210
    • Lustig, B.1    Fink, A.L.2
  • 7
    • 0028924676 scopus 로고
    • Thermal stability and CD analysis of rat tyrosine hydroxylase
    • Gahn, L. G.; Roskoski, R., Jr. Thermal stability and CD analysis of rat tyrosine hydroxylase. Biochemistry 1995, 34, 252-256.
    • (1995) Biochemistry , vol.34 , pp. 252-256
    • Gahn, L.G.1    Roskoski Jr., R.2
  • 8
    • 0015804006 scopus 로고
    • The conformational stability of ribosomal proteins L7 and L12 from E. coli. I. Circular dichroism study of the changes induced by ionic strength and solvents
    • Boublik, M.; Brot, N.; Weissbach, H. The conformational stability of ribosomal proteins L7 and L12 from E. coli. I. Circular dichroism study of the changes induced by ionic strength and solvents. Biopolymers 1973, 12, 2083-2092.
    • (1973) Biopolymers , vol.12 , pp. 2083-2092
    • Boublik, M.1    Brot, N.2    Weissbach, H.3
  • 9
    • 0028027707 scopus 로고
    • A kinetic method to evaluate the two-state character of solvent-induced protein denaturation
    • Mucke, M.; Schmid, F. X. A kinetic method to evaluate the two-state character of solvent-induced protein denaturation. Biochemistry 1994, 33, 12930-12935.
    • (1994) Biochemistry , vol.33 , pp. 12930-12935
    • Mucke, M.1    Schmid, F.X.2
  • 10
    • 0028826743 scopus 로고
    • Effects of ionic strength on the catalysis and stability of prolyl oligopeptidase
    • Polgar, L. Effects of ionic strength on the catalysis and stability of prolyl oligopeptidase. Biochem. J. 1995, 1312, 267-271.
    • (1995) Biochem. J , vol.1312 , pp. 267-271
    • Polgar, L.1
  • 11
    • 0029913459 scopus 로고    scopus 로고
    • Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration
    • Szeltner, Z.; Polgar, L. Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration. J. Biol. Chem. 1996, 271, 5458-5463.
    • (1996) J. Biol. Chem , vol.271 , pp. 5458-5463
    • Szeltner, Z.1    Polgar, L.2
  • 12
    • 0031042309 scopus 로고    scopus 로고
    • Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol
    • Hirota, N.; Mizuno, K.; Goto, Y. Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol. Protein Sci. 1997, 6, 416-421.
    • (1997) Protein Sci , vol.6 , pp. 416-421
    • Hirota, N.1    Mizuno, K.2    Goto, Y.3
  • 13
    • 0032536194 scopus 로고    scopus 로고
    • Group additive contributions to the alcohol-induced α-helix formation of melittin: Implication for the mechanism of the alcohol effects on proteins
    • Hirota, N.; Mizuno, K.; Goto, Y. Group additive contributions to the alcohol-induced α-helix formation of melittin: Implication for the mechanism of the alcohol effects on proteins. J. Mol. Biol. 1998, 275, 365-378.
    • (1998) J. Mol. Biol , vol.275 , pp. 365-378
    • Hirota, N.1    Mizuno, K.2    Goto, Y.3
  • 14
    • 0034573685 scopus 로고    scopus 로고
    • Time-dependent structure and activity changes of α-chymotrypsin in water/alcohol mixed solvents
    • Sato, M.; Sasaki, T.; Kobayashi, M.; Kise, H. Time-dependent structure and activity changes of α-chymotrypsin in water/alcohol mixed solvents. Biosci. Biotechnol. Biochem. 2000, 64, 2552-2558.
    • (2000) Biosci. Biotechnol. Biochem , vol.64 , pp. 2552-2558
    • Sato, M.1    Sasaki, T.2    Kobayashi, M.3    Kise, H.4
  • 16
    • 0030949636 scopus 로고    scopus 로고
    • Active conformation of α-chymotrypsin in organic solvents as studied by circular dichroism
    • Sasaki, T.; Kobayashi, M.; Kise, H. Active conformation of α-chymotrypsin in organic solvents as studied by circular dichroism. Biotechnol. Tech. 1997, 11, 387-390.
    • (1997) Biotechnol. Tech , vol.11 , pp. 387-390
    • Sasaki, T.1    Kobayashi, M.2    Kise, H.3
  • 17
    • 0031679652 scopus 로고    scopus 로고
    • Surface-induced changes in the structure and activity of enzymes physically immobilized at solid/liquid interfaces
    • Norde, W.; Zoungrana, T. Surface-induced changes in the structure and activity of enzymes physically immobilized at solid/liquid interfaces. Biotechnol. Appl. Biochem. 1998, 28, 133-143.
    • (1998) Biotechnol. Appl. Biochem , vol.28 , pp. 133-143
    • Norde, W.1    Zoungrana, T.2
  • 18
    • 0033150603 scopus 로고    scopus 로고
    • Conformational changes of fibrinogen adsorption onto hydroxyapatite and titanium oxide nanoparticles
    • Yongli, C.; Xiufang, Z.; Yandao, G.; Nanming, Z.; Tingying, Z.; Xinqi, S. Conformational changes of fibrinogen adsorption onto hydroxyapatite and titanium oxide nanoparticles. J. Colloid Interface Sci. 1999, 214, 38-45.
    • (1999) J. Colloid Interface Sci , vol.214 , pp. 38-45
    • Yongli, C.1    Xiufang, Z.2    Yandao, G.3    Nanming, Z.4    Tingying, Z.5    Xinqi, S.6
  • 19
    • 0028018145 scopus 로고
    • Organic-solvent-tolerant bacterium which secretes organic-solvent-stable lipolytic enzyme
    • Ogino, H.; Miyamoto, K.; Ishikawa, H. Organic-solvent-tolerant bacterium which secretes organic-solvent-stable lipolytic enzyme. Appl. Environ. Microbiol. 1994, 60, 3884-3886.
    • (1994) Appl. Environ. Microbiol , vol.60 , pp. 3884-3886
    • Ogino, H.1    Miyamoto, K.2    Ishikawa, H.3
  • 20
    • 0028808177 scopus 로고
    • Organic solvent-tolerant bacterium which secretes an organic solvent-stable proteolytic enzyme
    • Ogino, H.; Yasui, K.; Shiotani, T.; Ishihara, T.; Ishikawa, H. Organic solvent-tolerant bacterium which secretes an organic solvent-stable proteolytic enzyme. Appl. Environ. Microbiol. 1995, 61, 4258-4262.
    • (1995) Appl. Environ. Microbiol , vol.61 , pp. 4258-4262
    • Ogino, H.1    Yasui, K.2    Shiotani, T.3    Ishihara, T.4    Ishikawa, H.5
  • 21
    • 0033917914 scopus 로고    scopus 로고
    • Purification and characterization of organic solvent-stable lipase from organic solvent-tolerant Pseudomonas aeruginosa LST-03
    • Ogino, H.; Nakagawa, S.; Shinya, K.; Muto, T.; Fujimura, N.; Yasuda, M.; Ishikawa, H. Purification and characterization of organic solvent-stable lipase from organic solvent-tolerant Pseudomonas aeruginosa LST-03. J. Biosci. Bioeng. 2000, 89, 451-457.
    • (2000) J. Biosci. Bioeng , vol.89 , pp. 451-457
    • Ogino, H.1    Nakagawa, S.2    Shinya, K.3    Muto, T.4    Fujimura, N.5    Yasuda, M.6    Ishikawa, H.7
  • 22
    • 0032906896 scopus 로고    scopus 로고
    • Purification and characterization of organic solvent-stable protease from organic solvent-tolerant Pseudomonas aeruginosa PST-01
    • Ogino, H.; Watanabe, F.; Yamada, M.; Nakagawa, S.; Hirose, T.; Noguchi, A.; Yasuda, M.; Ishikawa, H. Purification and characterization of organic solvent-stable protease from organic solvent-tolerant Pseudomonas aeruginosa PST-01. J. Biosci. Bioeng. 1999, 87, 61-68.
    • (1999) J. Biosci. Bioeng , vol.87 , pp. 61-68
    • Ogino, H.1    Watanabe, F.2    Yamada, M.3    Nakagawa, S.4    Hirose, T.5    Noguchi, A.6    Yasuda, M.7    Ishikawa, H.8
  • 23
    • 0033428798 scopus 로고    scopus 로고
    • Peptide synthesis catalyzed by organic solvent-stable protease from Pseudomonas aeruginosa PST-01 in monophasic aqueous-organic solvent systems
    • Ogino, H.; Yamada, M.; Watanabe, F.; Ichinose, H.; Yasuda, M.; Ishikawa, H. Peptide synthesis catalyzed by organic solvent-stable protease from Pseudomonas aeruginosa PST-01 in monophasic aqueous-organic solvent systems. J. Biosci. Bioeng. 1999, 88, 513-518.
    • (1999) J. Biosci. Bioeng , vol.88 , pp. 513-518
    • Ogino, H.1    Yamada, M.2    Watanabe, F.3    Ichinose, H.4    Yasuda, M.5    Ishikawa, H.6
  • 24
    • 0034120419 scopus 로고    scopus 로고
    • The synthetic rate of dipeptide catalyzed by organic solvent-stable protease from Pseudomonas aeruginosa PST-01 in the presence of water-soluble organic solvents
    • Ogino, H.; Gemba, Y.; Yamada, M.; Shizuka, M.; Yasuda, M.; Ishikawa, H. The synthetic rate of dipeptide catalyzed by organic solvent-stable protease from Pseudomonas aeruginosa PST-01 in the presence of water-soluble organic solvents. Biochem. Eng. J. 2000, 5, 219-223.
    • (2000) Biochem. Eng. J , vol.5 , pp. 219-223
    • Ogino, H.1    Gemba, Y.2    Yamada, M.3    Shizuka, M.4    Yasuda, M.5    Ishikawa, H.6
  • 25
    • 2342419734 scopus 로고    scopus 로고
    • Kinetics and mechanism of a reaction catalyzed by PST-01 protease from Pseudomonas aeruginosa PST-01
    • Bobe, I. M.; Abdelmoez, W.; Ogino, H.; Yasuda, M.; Ishimi, K.; Ishikawa, H. Kinetics and mechanism of a reaction catalyzed by PST-01 protease from Pseudomonas aeruginosa PST-01. Biotechnol. Bioeng. 2004, 86, 365-373.
    • (2004) Biotechnol. Bioeng , vol.86 , pp. 365-373
    • Bobe, I.M.1    Abdelmoez, W.2    Ogino, H.3    Yasuda, M.4    Ishimi, K.5    Ishikawa, H.6
  • 26
    • 0034084383 scopus 로고    scopus 로고
    • Cloning and sequencing of a gene of organic solvent-stable protease secreted from Pseudomonas aeruginosa PST-01 and its expression in Escherichia coli
    • Ogino, H.; Yokoo, J.; Watanabe, F.; Ishikawa, H. Cloning and sequencing of a gene of organic solvent-stable protease secreted from Pseudomonas aeruginosa PST-01 and its expression in Escherichia coli. Biochem. Eng. J. 2000, 5, 191-200.
    • (2000) Biochem. Eng. J , vol.5 , pp. 191-200
    • Ogino, H.1    Yokoo, J.2    Watanabe, F.3    Ishikawa, H.4
  • 27
    • 0035140742 scopus 로고    scopus 로고
    • Role of intermolecular disulfide bonds of the organic solvent-stable PST-01 protease in the organic solvent-stability
    • Ogino, H.; Uchiho, T.; Yokoo, J.; Kobayashi, R.; Ichise, R.; Ishikawa, H. Role of intermolecular disulfide bonds of the organic solvent-stable PST-01 protease in the organic solvent-stability. Appl. Environ. Microbiol. 2001, 67, 942-947.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 942-947
    • Ogino, H.1    Uchiho, T.2    Yokoo, J.3    Kobayashi, R.4    Ichise, R.5    Ishikawa, H.6
  • 28
    • 0013349214 scopus 로고
    • New cotton effects in polypeptides and proteins
    • Blout, E. R.; Schmier, I.; Simmons, N. S. New cotton effects in polypeptides and proteins. J. Am. Chem. Soc. 1962, 84, 3193-3194.
    • (1962) J. Am. Chem. Soc , vol.84 , pp. 3193-3194
    • Blout, E.R.1    Schmier, I.2    Simmons, N.S.3
  • 29
    • 0000998310 scopus 로고
    • The optical activity of polypeptides in the far ultraviolet
    • Holzwarth, G.; Gratzer, W. B.; Doty, P. The optical activity of polypeptides in the far ultraviolet. J. Am. Chem. Soc. 1962, 84, 3194-3196.
    • (1962) J. Am. Chem. Soc , vol.84 , pp. 3194-3196
    • Holzwarth, G.1    Gratzer, W.B.2    Doty, P.3
  • 30
    • 11344291497 scopus 로고
    • The ultraviolet circular dichroism of polypeptides
    • Holzwarth, G.; Doty, P. The ultraviolet circular dichroism of polypeptides. J. Am. Chem. Soc. 1965, 87, 218-228.
    • (1965) J. Am. Chem. Soc , vol.87 , pp. 218-228
    • Holzwarth, G.1    Doty, P.2
  • 31
    • 0014227144 scopus 로고
    • New chain conformations of poly-(glutamic acid) and polylysine
    • Tiffany, M. L.; Krimm, S. New chain conformations of poly-(glutamic acid) and polylysine. Biopolymers 1968, 6, 1379-1382.
    • (1968) Biopolymers , vol.6 , pp. 1379-1382
    • Tiffany, M.L.1    Krimm, S.2
  • 32
    • 0013901785 scopus 로고
    • The optical rotatory properties of the β-configuration in polypeptides and proteins
    • Sarkar, P. K.; Doty, P. The optical rotatory properties of the β-configuration in polypeptides and proteins. Proc. Natl. Acad. Sci. U.S.A. 1966, 55, 981-989.
    • (1966) Proc. Natl. Acad. Sci. U.S.A , vol.55 , pp. 981-989
    • Sarkar, P.K.1    Doty, P.2
  • 33
    • 0014440288 scopus 로고
    • Circular dichroism of β-poly-L- lysine
    • Li, L.-K.; Spector, A. Circular dichroism of β-poly-L- lysine. J. Am. Chem. Soc. 1969, 97, 220-222.
    • (1969) J. Am. Chem. Soc , vol.97 , pp. 220-222
    • Li, L.-K.1    Spector, A.2
  • 34
    • 0000798347 scopus 로고
    • Intrinsic cotton effects in collagen and poly-L-proline
    • Blout, E. R.; Carver, J. P.; Gross, J. Intrinsic cotton effects in collagen and poly-L-proline. J. Am. Chem. Soc. 1963, 85, 644-646.
    • (1963) J. Am. Chem. Soc , vol.85 , pp. 644-646
    • Blout, E.R.1    Carver, J.P.2    Gross, J.3
  • 35
    • 0014378447 scopus 로고
    • Circular dichroism of poly-L-proline in an unordered conformation
    • Tiffany, M. L.; Krimm, S. Circular dichroism of poly-L-proline in an unordered conformation. Biopolymers 1968, 6, 1767-1770.
    • (1968) Biopolymers , vol.6 , pp. 1767-1770
    • Tiffany, M.L.1    Krimm, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.