메뉴 건너뛰기




Volumn 63, Issue 10, 1997, Pages 3985-3991

Pressure-enhanced activity and stability of a hyperthermophilic protease from a deep-sea methanogen

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; PROTEINASE;

EID: 0030773807     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.63.10.3985-3991.1997     Document Type: Article
Times cited : (67)

References (44)
  • 1
    • 0006834110 scopus 로고
    • Microbial life at high temperatures: Mechanisms and molecular aspects
    • D. J. Kushner (ed.), Springer-Verlag, New York, N.Y.
    • Amelunxen, R. E., and A. L. Murdock. 1978. Microbial life at high temperatures: mechanisms and molecular aspects, p. 217-278. In D. J. Kushner (ed.), Microbial life in extreme environments. Springer-Verlag, New York, N.Y.
    • (1978) Microbial Life in Extreme Environments , pp. 217-278
    • Amelunxen, R.E.1    Murdock, A.L.2
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
  • 4
    • 14644421094 scopus 로고    scopus 로고
    • Protein engineering for stability
    • J. Cleland and C. S. Craik (ed.). Wiley-Liss, New York, N.Y.
    • Braxton, S. 1996. Protein engineering for stability, p. 299-316. In J. Cleland and C. S. Craik (ed.). Protein engineering. Wiley-Liss, New York, N.Y.
    • (1996) Protein Engineering , pp. 299-316
    • Braxton, S.1
  • 5
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii
    • Bult, C. J., et al. 1996. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273:1058-1073.
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1
  • 6
    • 0026707185 scopus 로고
    • A heat stable serine protease from the extremely thermophilic archaebacterium Sulfolobus solfataricus
    • Burlini, N., P. Magnani, A. Villa, F. Macchi, P. Tortora, and A. Guerritore. 1992. A heat stable serine protease from the extremely thermophilic archaebacterium Sulfolobus solfataricus. Biochim. Biophys. Acta 1122:283-292.
    • (1992) Biochim. Biophys. Acta , vol.1122 , pp. 283-292
    • Burlini, N.1    Magnani, P.2    Villa, A.3    Macchi, F.4    Tortora, P.5    Guerritore, A.6
  • 7
    • 84957363672 scopus 로고
    • A colorometric method for the determination of the proteolytic activity of duodenal juice
    • Charney, J., and R. M. Tomarelli. 1947. A colorometric method for the determination of the proteolytic activity of duodenal juice. J. Biol. Chem. 171:501-505.
    • (1947) J. Biol. Chem. , vol.171 , pp. 501-505
    • Charney, J.1    Tomarelli, R.M.2
  • 8
    • 0020479358 scopus 로고
    • Purification and some properties of an extracellular protease (Caldolysin) from an extreme thermophile
    • Cowan, D. A., and R. M. Daniel. 1982. Purification and some properties of an extracellular protease (Caldolysin) from an extreme thermophile. Biochim. Biophys. Acta 705:293-305.
    • (1982) Biochim. Biophys. Acta , vol.705 , pp. 293-305
    • Cowan, D.A.1    Daniel, R.M.2
  • 9
    • 0023069360 scopus 로고
    • The specific activities of mesophilic and thermophilic proteinases
    • Cowan, D. A., R. M. Daniel, and H. W. Morgan. 1987. The specific activities of mesophilic and thermophilic proteinases. Int. J. Biochem. 19:741-743.
    • (1987) Int. J. Biochem. , vol.19 , pp. 741-743
    • Cowan, D.A.1    Daniel, R.M.2    Morgan, H.W.3
  • 10
    • 0023425517 scopus 로고
    • An extremely thermostable extracellular proteinase from a strain of the archaebacterium Desulfurococcus growing at 88°C
    • 24719
    • Cowan, D. A., K. A. Smolenski, R. M. Daniel, and H. W. Morgan. 1987. An extremely thermostable extracellular proteinase from a strain of the archaebacterium Desulfurococcus growing at 88°C. Biochem. J. 24719:121-133.
    • (1987) Biochem. J. , pp. 121-133
    • Cowan, D.A.1    Smolenski, K.A.2    Daniel, R.M.3    Morgan, H.W.4
  • 11
    • 0025088034 scopus 로고
    • Characterization of pyrolysin, a hyperthermophilic serine protease from the archaebacterium Pyrococcus furiosus
    • Eggen, R., A. Geerling, J. Watts, and W. M. de Vos. 1990. Characterization of pyrolysin, a hyperthermophilic serine protease from the archaebacterium Pyrococcus furiosus. FEMS Microbiol. Lett. 71:17-20.
    • (1990) FEMS Microbiol. Lett. , vol.71 , pp. 17-20
    • Eggen, R.1    Geerling, A.2    Watts, J.3    De Vos, W.M.4
  • 12
    • 0001834289 scopus 로고
    • How nature engineers protein (thermo)stability
    • G. di Prisco (ed.), Springer-Verlag, Berlin, Germany
    • Fontana, A. 1991. How nature engineers protein (thermo)stability, p. 89-113. In G. di Prisco (ed.), Life under extreme conditions. Springer-Verlag, Berlin, Germany.
    • (1991) Life under Extreme Conditions , pp. 89-113
    • Fontana, A.1
  • 13
    • 0342408718 scopus 로고
    • Laboratory of Biological Chemistry, College of Agriculture, University of Osaka Prefecture, Osaka, Japan
    • Fukuda, H., and K. Takahashi. 1987. Temperature dependence of buffer pH/pKa. Laboratory of Biological Chemistry, College of Agriculture, University of Osaka Prefecture, Osaka, Japan.
    • (1987) Temperature Dependence of Buffer PH/pKa
    • Fukuda, H.1    Takahashi, K.2
  • 14
    • 0025171939 scopus 로고
    • Isolation and characterization of an intracellular aminopeptidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus
    • Hanner, M., B. Redl, and G. Stoffler. 1990. Isolation and characterization of an intracellular aminopeptidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus. Biochim. Biophys. Acta 1033:148-153.
    • (1990) Biochim. Biophys. Acta , vol.1033 , pp. 148-153
    • Hanner, M.1    Redl, B.2    Stoffler, G.3
  • 15
    • 0024970964 scopus 로고
    • Catalytic properties of thermophilic lactate dehydrogenase and halophilic malate dehydrogenase at high temperatures and low water activity
    • Hecht, K., K. Wrba, and R. Jaenicke. 1989. Catalytic properties of thermophilic lactate dehydrogenase and halophilic malate dehydrogenase at high temperatures and low water activity. Eur. J. Biochem. 183:69-74.
    • (1989) Eur. J. Biochem. , vol.183 , pp. 69-74
    • Hecht, K.1    Wrba, K.2    Jaenicke, R.3
  • 16
    • 0028217082 scopus 로고
    • Pressure stabilization of proteins from extreme thermophiles
    • Hei, D. J., and D. S. Clark. 1994. Pressure stabilization of proteins from extreme thermophiles. Appl. Environ. Microbiol. 60:932-939.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 932-939
    • Hei, D.J.1    Clark, D.S.2
  • 17
    • 0021312844 scopus 로고
    • Detection and characterization of epidermal proteinases by polyacrylamide gel electrophoresis
    • Horie, N., K. Fukuyama, Y. Ito, and W. L. Epstein. 1984. Detection and characterization of epidermal proteinases by polyacrylamide gel electrophoresis. Comp. Biochem. Physiol. B 77:349-353.
    • (1984) Comp. Biochem. Physiol. B , vol.77 , pp. 349-353
    • Horie, N.1    Fukuyama, K.2    Ito, Y.3    Epstein, W.L.4
  • 18
    • 0029008010 scopus 로고    scopus 로고
    • Discovering novel bacteria with an eye to biotechnological applications
    • Horikoshi, K. 1996. Discovering novel bacteria with an eye to biotechnological applications. Curr. Biol. 6:292-297.
    • (1996) Curr. Biol. , vol.6 , pp. 292-297
    • Horikoshi, K.1
  • 19
    • 0023038088 scopus 로고
    • A new way of enhancing the thermostability of proleases
    • Imanaka, T., M. Shibagaki, and M. Tagaki. 1986. A new way of enhancing the thermostability of proleases. Nature 324:695-697.
    • (1986) Nature , vol.324 , pp. 695-697
    • Imanaka, T.1    Shibagaki, M.2    Tagaki, M.3
  • 20
    • 0021070752 scopus 로고
    • Methanococcus jannaschii sp. nov., an extremely thermophilic methanogen from a submarine hydrothermal vent
    • Jones, W., A. Leigh, F. Mayer, C. Woese, and R. Wolfe. 1983. Methanococcus jannaschii sp. nov., an extremely thermophilic methanogen from a submarine hydrothermal vent. Arch. Microbiol. 136:254-261.
    • (1983) Arch. Microbiol. , vol.136 , pp. 254-261
    • Jones, W.1    Leigh, A.2    Mayer, F.3    Woese, C.4    Wolfe, R.5
  • 21
    • 0029670677 scopus 로고    scopus 로고
    • Glycine 15 in the bend between two-helices can enhance the thermostability of DNA binding protein HU from Bacillus stearothermophilus
    • Kawamura, S., Y. Kakuta, I. Tanaka, K. Hikichi, S. Kuhara, N. Yamasaki, and N. Kimura. 1996. Glycine 15 in the bend between two-helices can enhance the thermostability of DNA binding protein HU from Bacillus stearothermophilus. Biochemistry 35:1195-1200.
    • (1996) Biochemistry , vol.35 , pp. 1195-1200
    • Kawamura, S.1    Kakuta, Y.2    Tanaka, I.3    Hikichi, K.4    Kuhara, S.5    Yamasaki, N.6    Kimura, N.7
  • 22
    • 0013647027 scopus 로고
    • Characterization of enzymes from high-temperature bacteria
    • M. W. W. Adams and R. M. Kelly (ed.), American Chemical Society, Washington, D.C.
    • Kelly, R. M., S. H. Brown, I. I. Blumenthals, and M. W. W. Adams. 1992. Characterization of enzymes from high-temperature bacteria, p. 23-41. In M. W. W. Adams and R. M. Kelly (ed.), Biocatalysis at extreme temperatures, vol. 498. American Chemical Society, Washington, D.C.
    • (1992) Biocatalysis at Extreme Temperatures , vol.498 , pp. 23-41
    • Kelly, R.M.1    Brown, S.H.2    Blumenthals, I.I.3    Adams, M.W.W.4
  • 23
    • 0000429832 scopus 로고
    • Application of high pressure technology to food processing
    • Knorr, D. 1993. Application of high pressure technology to food processing. Food Technol. 47(6):156-161.
    • (1993) Food Technol. , vol.47 , Issue.6 , pp. 156-161
    • Knorr, D.1
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0023248340 scopus 로고
    • Effect of pressure on the pre-steady-state kinetics of the hydrolysis of anilide substrates catalyzed by α-chymotrypsin
    • Makimoto, S., and Y. Taniguchi. 1987. Effect of pressure on the pre-steady-state kinetics of the hydrolysis of anilide substrates catalyzed by α-chymotrypsin. Biochim. Biophys. Acta 914:304-307.
    • (1987) Biochim. Biophys. Acta , vol.914 , pp. 304-307
    • Makimoto, S.1    Taniguchi, Y.2
  • 26
    • 0002639249 scopus 로고
    • Production of thermophilic extracellular proteases (aqualysins I and II) by Thermus aquaticus TY-1, an extreme thermophile
    • Matsuzawa, H., M. Hamaoki, and T. Ohta. 1983. Production of thermophilic extracellular proteases (aqualysins I and II) by Thermus aquaticus TY-1, an extreme thermophile. Agric. Biol. Chem. 47:25-29.
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 25-29
    • Matsuzawa, H.1    Hamaoki, M.2    Ohta, T.3
  • 27
    • 0030156252 scopus 로고    scopus 로고
    • A hyperthermophilic protease of the subtilisin family bound to the surface layer of the archaeon Staphylothermus marinus
    • Mayr, J., A. Lupas, J. Kellermenn, C. Eckerskorn, W. Baumeister, and J. Peters. 1996. A hyperthermophilic protease of the subtilisin family bound to the surface layer of the archaeon Staphylothermus marinus. Curr. Biol. 6(6): 739-749.
    • (1996) Curr. Biol. , vol.6 , Issue.6 , pp. 739-749
    • Mayr, J.1    Lupas, A.2    Kellermenn, J.3    Eckerskorn, C.4    Baumeister, W.5    Peters, J.6
  • 28
    • 0011098198 scopus 로고
    • Pressure dependence of enzyme catalysis
    • M. W. W. Adams and R. M. Kelly (ed.), American Chemical Society, Washington, D.C.
    • Michels, P. C., and D. S. Clark. 1992. Pressure dependence of enzyme catalysis, p. 1088-121. In M. W. W. Adams and R. M. Kelly (ed.), Biocatalysis at extreme temperatures, vol. 498. American Chemical Society, Washington, D.C.
    • (1992) Biocatalysis at Extreme Temperatures , vol.498 , pp. 1088-1121
    • Michels, P.C.1    Clark, D.S.2
  • 29
    • 0029832690 scopus 로고    scopus 로고
    • Pressure effects on enzyme activity and stability at high temperatures
    • Michels, P. C., D. Hei, and D. S. Clark. 1996. Pressure effects on enzyme activity and stability at high temperatures. Adv. Protein Chem. 48:341-376.
    • (1996) Adv. Protein Chem. , vol.48 , pp. 341-376
    • Michels, P.C.1    Hei, D.2    Clark, D.S.3
  • 30
    • 0024962539 scopus 로고
    • High Pressure-temperature bioreactor: Assays of thermostable hydrogenase with fiber optics
    • Miller, J. F., C. M. Nelson, J. M. Ludlow, N. N. Shah, and D. S. Clark. 1989. High Pressure-temperature bioreactor: assays of thermostable hydrogenase with fiber optics. Biotechnol. Bioeng. 34:1015-1021.
    • (1989) Biotechnol. Bioeng. , vol.34 , pp. 1015-1021
    • Miller, J.F.1    Nelson, C.M.2    Ludlow, J.M.3    Shah, N.N.4    Clark, D.S.5
  • 31
    • 0000519053 scopus 로고
    • Pressure and temperature effects on growth and methane production of the extreme thermophile Methanococcus jannaschii
    • Miller, J. F., C. M. Nelson, N. N. Shah, J. M. Ludlow, and D. S. Clark. 1988. Pressure and temperature effects on growth and methane production of the extreme thermophile Methanococcus jannaschii. Appl. Environ. Microbiol. 54:3039-3042.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 3039-3042
    • Miller, J.F.1    Nelson, C.M.2    Shah, N.N.3    Ludlow, J.M.4    Clark, D.S.5
  • 32
    • 0015523878 scopus 로고
    • A comparative study of spinlabelled serine enzymes: Acetylcholinesterase, trypsin, chymotrypsin, elastase, and subtilisin
    • Morrisett, J. D., and C. A. Broomfield. 1972. A comparative study of spinlabelled serine enzymes: acetylcholinesterase, trypsin, chymotrypsin, elastase, and subtilisin. J. Biol. Chem. 247:7224-7231.
    • (1972) J. Biol. Chem. , vol.247 , pp. 7224-7231
    • Morrisett, J.D.1    Broomfield, C.A.2
  • 33
    • 0025022699 scopus 로고
    • Protein engineering for thermostability
    • Nosoh, Y., and T. Sekiguchi. 1990. Protein engineering for thermostability. Trends Biotechnol. 8:16-20.
    • (1990) Trends Biotechnol. , vol.8 , pp. 16-20
    • Nosoh, Y.1    Sekiguchi, T.2
  • 34
    • 0028986679 scopus 로고
    • Thermal stability of chimeric isoproylmalate dehydrogenase genes constructed from a mesophile and a thermophile
    • Numata, K., M. Muro, N. Akutsu, Y. Nosoh, A. Yamagishi, and T. Oshima. 1995. Thermal stability of chimeric isoproylmalate dehydrogenase genes constructed from a mesophile and a thermophile. Protein Eng. 8:39-43.
    • (1995) Protein Eng. , vol.8 , pp. 39-43
    • Numata, K.1    Muro, M.2    Akutsu, N.3    Nosoh, Y.4    Yamagishi, A.5    Oshima, T.6
  • 35
    • 0026112861 scopus 로고
    • Isolation and partial characterization of a novel thermostable carboxylesterase from a thermophilic Bacillus
    • Owusu, R. K., and D. A. Cowan. 1991. Isolation and partial characterization of a novel thermostable carboxylesterase from a thermophilic Bacillus. Enzyme Microb. Technol. 13:158-163.
    • (1991) Enzyme Microb. Technol. , vol.13 , pp. 158-163
    • Owusu, R.K.1    Cowan, D.A.2
  • 36
  • 37
    • 0002006941 scopus 로고
    • Inhibition of proteolytic enzymes
    • R. J. Beynon and J. S. Bond (ed.), IRL Press, Oxford, England
    • Salvesen, G., and H. Nagase. 1989. Inhibition of proteolytic enzymes, p. 83-105. In R. J. Beynon and J. S. Bond (ed.), Proteolytic enzymes: a practical approach. IRL Press, Oxford, England.
    • (1989) Proteolytic Enzymes: a Practical Approach , pp. 83-105
    • Salvesen, G.1    Nagase, H.2
  • 39
    • 0024728590 scopus 로고
    • Caldolase, a chelator-insensitive extracellular serine proteinase from a Thermus sp
    • Saravani, G.-A., D. A. Cowan, R. M. Daniel, and H. W. Morgan. 1989. Caldolase, a chelator-insensitive extracellular serine proteinase from a Thermus sp. Biochem. J. 262:409-416.
    • (1989) Biochem. J. , vol.262 , pp. 409-416
    • Saravani, G.-A.1    Cowan, D.A.2    Daniel, R.M.3    Morgan, H.W.4
  • 40
    • 0028982269 scopus 로고
    • Construction of chimeric beta glucosidases with improved enzymic properties
    • Singh, A., and K. Hayashi. 1995. Construction of chimeric beta glucosidases with improved enzymic properties. J. Biol. Chem. 270:21928-21933.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21928-21933
    • Singh, A.1    Hayashi, K.2
  • 41
    • 0342408714 scopus 로고
    • Characterization of extracellular protease activity from Thermus caldophilus GK24
    • Taguchi, H., M. Hamaoki, H. Matsugawa, and T. Ohta. 1983. Characterization of extracellular protease activity from Thermus caldophilus GK24. J. Biochem. 93:1983.
    • (1983) J. Biochem. , vol.93 , pp. 1983
    • Taguchi, H.1    Hamaoki, M.2    Matsugawa, H.3    Ohta, T.4
  • 42
    • 0028014671 scopus 로고
    • Continuous culture of Methanococcus jannaschii, an extremely thermophilic methanogen
    • Tsao, J.-H., S. M. Kaneshiro, S. Yu, and D. S. Clark. 1994. Continuous culture of Methanococcus jannaschii, an extremely thermophilic methanogen. Biotechnol. Bioeng. 43:258-261.
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 258-261
    • Tsao, J.-H.1    Kaneshiro, S.M.2    Yu, S.3    Clark, D.S.4
  • 43
    • 33845184910 scopus 로고
    • Activation and reaction volumes in solution
    • van Eldik, R., T. Asano, and W. J. Le Noble. 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
  • 44
    • 0028095184 scopus 로고
    • The sequence of a subtilisin-type protease (aerolysin) from the hyperthermophilic archaeum Pyrobaculum aerophilum reveals sites important to thermostability
    • J.
    • Volkl, P., P. Markiewicz, K. O. Stetter, J. and Miller. 1994. The sequence of a subtilisin-type protease (aerolysin) from the hyperthermophilic archaeum Pyrobaculum aerophilum reveals sites important to thermostability. Protein Sci. 3:1329-1340.
    • (1994) Protein Sci. , vol.3 , pp. 1329-1340
    • Volkl, P.1    Markiewicz, P.2    Stetter, K.O.3    Miller4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.