메뉴 건너뛰기




Volumn 98, Issue 18, 2014, Pages 7825-7836

An intermolecular disulfide bond is required for thermostability and thermoactivity of β-glycosidase from Thermococcus kodakarensis KOD1

Author keywords

Cysteine residues; Disulfide bond; Thermoactivity; Thermostability; glycosidase

Indexed keywords

AMINO ACIDS; COVALENT BONDS; ENZYMES; SULFUR COMPOUNDS;

EID: 84906944766     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-5731-6     Document Type: Article
Times cited : (10)

References (51)
  • 1
    • 0031554925 scopus 로고    scopus 로고
    • Crystal structure of the β-glycosidase from the hyperthermophilic archeon sulfolobus solfataricus: Resilience as a key factor in thermostability
    • DOI 10.1006/jmbi.1997.1215
    • Aguilar CF, Sanderson I, Moracci M, Ciaramella M, Nucci R, Rossi M, Pearl LH (1997) Crystal structure of the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability. J Mol Biol 271(5):789-802. doi:10.1006/jmbi.1997.1215 (Pubitemid 27376054)
    • (1997) Journal of Molecular Biology , vol.271 , Issue.5 , pp. 789-802
    • Aguilar, C.F.1    Sanderson, I.2    Moracci, M.3    Ciaramella, M.4    Nucci, R.5    Rossi, M.6    Pearl, L.H.7
  • 2
    • 84893023329 scopus 로고    scopus 로고
    • A novel maltotriose hydrolyzing thermo-acidophilic pullulan hydrolase type III from Thermococcus kodakarensis
    • doi:10.1128/AEM.03139-13
    • Ahmad N, Rashid N, Haider MS, Akram M, Akhtar M (2013) A novel maltotriose hydrolyzing thermo-acidophilic pullulan hydrolase type III from Thermococcus kodakarensis. Appl Environ Microbiol. doi:10.1128/AEM.03139-13
    • (2013) Appl Environ Microbiol
    • Ahmad, N.1    Rashid, N.2    Haider, M.S.3    Akram, M.4    Akhtar, M.5
  • 3
    • 10344266893 scopus 로고
    • Alteration of the kinetic properties of an enzyme by the binding of buffer, inhibitor, or substrate
    • Alberty RA, Bock RM (1953) Alteration of the kinetic properties of an enzyme by the binding of buffer, inhibitor, or substrate. Proc Natl Acad Sci U S A 39(9):895-900
    • (1953) Proc Natl Acad Sci U S a , vol.39 , Issue.9 , pp. 895-900
    • Alberty, R.A.1    Bock, R.M.2
  • 4
    • 8444239349 scopus 로고    scopus 로고
    • Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1
    • Atomi H, Fukui T, Kanai T, Morikawa M, Imanaka T (2004) Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1. Archaea 1(4):263-267. doi:10.1155/2004/204953 (Pubitemid 39520708)
    • (2004) Archaea , vol.1 , Issue.4 , pp. 263-267
    • Atomi, H.1    Fukui, T.2    Kanai, T.3    Morikawa, M.4    Imanaka, T.5
  • 5
    • 80053385099 scopus 로고    scopus 로고
    • Application of hyperthermophiles and their enzymes
    • doi:10.1016/j.copbio.2011.06.010
    • Atomi H, Sato T, Kanai T (2011) Application of hyperthermophiles and their enzymes. Curr Opin Biotechnol 22(5):618-626. doi:10.1016/j.copbio.2011.06. 010
    • (2011) Curr Opin Biotechnol , vol.22 , Issue.5 , pp. 618-626
    • Atomi, H.1    Sato, T.2    Kanai, T.3
  • 6
    • 0036448608 scopus 로고    scopus 로고
    • Microbial β-glucosidases: Cloning, properties, and applications
    • DOI 10.1080/07388550290789568
    • Bhatia Y, Mishra S, Bisaria VS (2002) Microbial beta-glucosidases: cloning, properties, and applications. Crit Rev Biotechnol 22(4):375-407. doi:10.1080/07388550290789568 (Pubitemid 35446303)
    • (2002) Critical Reviews in Biotechnology , vol.22 , Issue.4 , pp. 375-407
    • Bhatia, Y.1    Mishra, S.2    Bisaria, V.S.3
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgramquantities of protein utilizing the principle of protein-dye binding
    • doi:10.1016/0003-2697(76)90527-3
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgramquantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254. doi:10.1016/0003-2697(76)90527-3
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0037424370 scopus 로고    scopus 로고
    • Activity-stability relationships in extremophilic enzymes
    • DOI 10.1074/jbc.M212508200
    • D'Amico S, Marx J-C, Gerday C, Feller G (2003) Activity-stability relationships in extremophilic enzymes. J Biol Chem 278(10):7891-7896. doi:10.1074/jbc.M212508200 (Pubitemid 36800524)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 7891-7896
    • D'Amico, S.1    Marx, J.-C.2    Gerday, C.3    Feller, G.4
  • 10
    • 33745935761 scopus 로고    scopus 로고
    • Industrial applications of hyperthermophilic enzymes: A review
    • DOI 10.2174/092986606777790548
    • de Miguel Bouzas T, Barros-Velazquez J, Villa TG (2006) Industrial applications of hyperthermophilic enzymes: a review. Protein Pept Lett 13(7):645-651. doi:10.2174/092986606777790548 (Pubitemid 44055782)
    • (2006) Protein and Peptide Letters , vol.13 , Issue.7 , pp. 645-651
    • De Miguel, B.T.1    Barros-Velazquez, J.2    Villa, T.G.3
  • 11
    • 27844584367 scopus 로고    scopus 로고
    • Industrial relevance of thermophilic Archaea
    • DOI 10.1016/j.mib.2005.10.015, PII S1369527405001712, Growth Development
    • Egorova K, Antranikian G (2005) Industrial relevance of thermophilic Archaea. Curr Opin Microbiol 8(6):649-655. doi:10.1016/j.mib.2005.10.015 (Pubitemid 41643962)
    • (2005) Current Opinion in Microbiology , vol.8 , Issue.6 , pp. 649-655
    • Egorova, K.1    Antranikian, G.2
  • 12
    • 0032573431 scopus 로고    scopus 로고
    • The stability of salt bridges at high temperatures: Implications for hyperthermophilic proteins
    • doi:10.1006/jmbi.1998.2159
    • Elcock AH (1998) The stability of salt bridges at high temperatures: Implications for hyperthermophilic proteins. J Mol Biol 284(2):489-502. doi:10.1006/jmbi.1998.2159
    • (1998) J Mol Biol , vol.284 , Issue.2 , pp. 489-502
    • Elcock, A.H.1
  • 13
    • 84859420715 scopus 로고    scopus 로고
    • Kinetic and thermodynamic characterization of the functional properties of a hybrid versatile peroxidase using isothermal titration calorimetry: Insight into manganese peroxidase activation and lignin peroxidase inhibition
    • doi:10.1016/j.biochi.2012.02.012
    • Ertan H, Siddiqui KS, Muenchhoff J, Charlton T, Cavicchioli R (2012) Kinetic and thermodynamic characterization of the functional properties of a hybrid versatile peroxidase using isothermal titration calorimetry: insight into manganese peroxidase activation and lignin peroxidase inhibition. Biochimie 94(5):1221-1231. doi:10.1016/j.biochi.2012.02.012
    • (2012) Biochimie , vol.94 , Issue.5 , pp. 1221-1231
    • Ertan, H.1    Siddiqui, K.S.2    Muenchhoff, J.3    Charlton, T.4    Cavicchioli, R.5
  • 15
    • 0034636975 scopus 로고    scopus 로고
    • Crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus
    • doi:10.1006/jmbi.2000.3977
    • Feese MD, Kato Y, Tamada T, Kato M, Komeda T, Miura Y, Hirose M, Hondo K, Kobayashi K, Kuroki R (2000) Crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus. J Mol Biol 301(2):451-464. doi:10.1006/jmbi.2000.3977
    • (2000) J Mol Biol , vol.301 , Issue.2 , pp. 451-464
    • Feese, M.D.1    Kato, Y.2    Tamada, T.3    Kato, M.4    Komeda, T.5    Miura, Y.6    Hirose, M.7    Hondo, K.8    Kobayashi, K.9    Kuroki, R.10
  • 16
    • 0346461016 scopus 로고    scopus 로고
    • SDS-resistant active and thermostable dimers are obtained from the dissociation of homotetrameric β-glycosidase from hyperthermophilic Sulfolobus solfataricus in SDS: Stabilizing role of the A-C intermonomeric interface
    • DOI 10.1074/jbc.M206761200
    • Gentile F, Amodeo P, Febbraio F, Picaro F, Motta A, Formisano S, Nucci R (2002) SDS-resistant active and thermostable dimers are obtained from the dissociation of homotetrameric beta-glycosidase from hyperthermophilic Sulfolobus solfataricus in SDS - stabilizing role of the A-C intermonomeric interface. J Biol Chem 277(46):44050-44060. doi:10.1074/jbc.M206761200 (Pubitemid 36157832)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.46 , pp. 44050-44060
    • Gentile, F.1    Amodeo, P.2    Febbraio, F.3    Picaro, F.4    Motta, A.5    Formisano, S.6    Nucci, R.7
  • 18
    • 0029166485 scopus 로고
    • Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases
    • Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G (1995) Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc Natl Acad Sci U S A 92(15):7090-7094
    • (1995) Proc Natl Acad Sci U S A , vol.92 , Issue.15 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.P.5    Davies, G.6
  • 19
    • 0037397499 scopus 로고    scopus 로고
    • Disulfide bonds as switches for protein function
    • doi:10.1016/S0968-0004(03)00057-4
    • Hogg PJ (2003) Disulfide bonds as switches for protein function. Trends Biochem Sci 28(4):210-214. doi:10.1016/S0968-0004(03)00057-4
    • (2003) Trends Biochem Sci , vol.28 , Issue.4 , pp. 210-214
    • Hogg, P.J.1
  • 21
    • 79959561821 scopus 로고    scopus 로고
    • Biochemical characterization of deblocking aminopeptidases from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1
    • doi:10.1271/bbb.110114
    • Jia B, Lee S, Pham BP, Kwack JM, Jin H, Li J, Wang Y, Cheong GW (2011) Biochemical characterization of deblocking aminopeptidases from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1. Biosci Biotechnol Biochem 75(6):1160-1166. doi:10.1271/bbb.110114
    • (2011) Biosci Biotechnol Biochem , vol.75 , Issue.6 , pp. 1160-1166
    • Jia, B.1    Lee, S.2    Pham, B.P.3    Kwack, J.M.4    Jin, H.5    Li, J.6    Wang, Y.7    Cheong, G.W.8
  • 22
    • 81555199788 scopus 로고    scopus 로고
    • Widespread disulfide bonding in proteins from thermophilic archaea
    • doi:10.1155/2011/409156
    • Jorda J, Yeates TO (2011) Widespread disulfide bonding in proteins from thermophilic archaea. Archaea 2011:409156. doi:10.1155/2011/409156
    • (2011) Archaea , vol.2011 , pp. 409156
    • Jorda, J.1    Yeates, T.O.2
  • 23
    • 83055169821 scopus 로고    scopus 로고
    • Structure of hyperthermophilic beta-glucosidase from Pyrococcus furiosus
    • doi:10.1107/S1744309111035238
    • Kado Y, Inoue T, Ishikawa K (2011) Structure of hyperthermophilic beta-glucosidase from Pyrococcus furiosus. Acta Crystallogr Sect F: Struct Biol Cryst Commun 67(12):1473 - 1479. doi:10.1107/S1744309111035238
    • (2011) Acta Crystallogr Sect F: Struct Biol Cryst Commun , vol.67 , Issue.12 , pp. 1473-1479
    • Kado, Y.1    Inoue, T.2    Ishikawa, K.3
  • 24
    • 84879506774 scopus 로고    scopus 로고
    • The role of disulfide bond in hyperthermophilic endocellulase
    • doi:10.1007/s00792-013-0542-8
    • Kim HW, Ishikawa K (2013) The role of disulfide bond in hyperthermophilic endocellulase. Extremophiles 17(4):593-599. doi:10.1007/s00792-013-0542-8
    • (2013) Extremophiles , vol.17 , Issue.4 , pp. 593-599
    • Kim, H.W.1    Ishikawa, K.2
  • 25
    • 77957963055 scopus 로고    scopus 로고
    • Achieving reliability and high accuracy in automated protein docking: ClusPro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19
    • doi:10.1002/prot.22835
    • Kozakov D, Hall DR, Beglov D, Brenke R, Comeau SR, Shen Y, Li K, Zheng J, Vakili P, Paschalidis I, Vajda S (2010) Achieving reliability and high accuracy in automated protein docking: ClusPro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19. Proteins 78(15):3124-3130. doi:10.1002/prot.22835
    • (2010) Proteins , vol.78 , Issue.15 , pp. 3124-3130
    • Kozakov, D.1    Hall, D.R.2    Beglov, D.3    Brenke, R.4    Comeau, S.R.5    Shen, Y.6    Li, K.7    Zheng, J.8    Vakili, P.9    Paschalidis, I.10    Vajda, S.11
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • doi:10.1038/227680a0
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227(5259):680-685. doi:10.1038/227680a0
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 84856984996 scopus 로고    scopus 로고
    • Characterization of a thermostable beta-glucosidase from Aspergillus fumigatus Z5, and its functional expression in Pichia pastoris X33
    • doi:10.1186/1475-2859-11-25
    • Liu DY, Zhang RF, Yang XM, Zhang ZH, Song S, Miao YZ, Shen QR (2012) Characterization of a thermostable beta-glucosidase from Aspergillus fumigatus Z5, and its functional expression in Pichia pastoris X33. Microb Cell Fact 11:25. doi:10.1186/1475-2859-11-25
    • (2012) Microb Cell Fact , vol.11 , pp. 25
    • Liu, D.Y.1    Zhang, R.F.2    Yang, X.M.3    Zhang, Z.H.4    Song, S.5    Miao, Y.Z.6    Shen, Q.R.7
  • 29
    • 0030706011 scopus 로고    scopus 로고
    • Kinetic and thermodynamic parameters for heat denaturation of bovine milk IgG, IgA and IgM
    • Mainer G, Sanchez L, Ena JM, Calvo M (1997) Kinetic and thermodynamic parameters for heat denaturation of bovine milk IgG, IgA and IgM. J Food Sci 62(5):1034-1038. doi:10.1111/j.1365-2621.1997.tb15032.x (Pubitemid 27463824)
    • (1997) Journal of Food Science , vol.62 , Issue.5 , pp. 1034-1038
    • Mainer, G.1    Sanchez, L.2    Ena, J.M.3    Calvo, M.4
  • 31
    • 34447313904 scopus 로고    scopus 로고
    • The stability of engineered thermostable neutral proteases from Bacillus stearothermophilus in organic solvents and detergents
    • DOI 10.1002/bit.21292
    • Mansfeld J, Ulbrich-Hofmann R (2007) The stability of engineered thermostable neutral proteases from Bacillus stearothermophilus in organic solvents and detergents. Biotechnol Bioeng 97(4):672-679. doi:10.1002/bit.21292 (Pubitemid 47051037)
    • (2007) Biotechnology and Bioengineering , vol.97 , Issue.4 , pp. 672-679
    • Mansfeld, J.1    Ulbrich-Hofmann, R.2
  • 32
    • 0024972502 scopus 로고
    • Substantial increase of protein stability by multiple disulphide bonds
    • doi:10.1038/342291a0
    • Matsumura M, Signor G, Matthews BW (1989) Substantial increase of protein stability by multiple disulphide bonds. Nature 342(6247):291-293. doi:10.1038/342291a0
    • (1989) Nature , vol.342 , Issue.6247 , pp. 291-293
    • Matsumura, M.1    Signor, G.2    Matthews, B.W.3
  • 33
    • 33748781976 scopus 로고    scopus 로고
    • Tools for integrated sequence-structure analysis with UCSF Chimera
    • doi:10.1186/1471-2105-7-339
    • Meng EC, Pettersen EF, Couch GS, Huang CC, Ferrin TE (2006) Tools for integrated sequence-structure analysis with UCSF Chimera. BMC Bioinforma 7:339. doi:10.1186/1471-2105-7-339
    • (2006) BMC Bioinforma , vol.7 , pp. 339
    • Meng, E.C.1    Pettersen, E.F.2    Couch, G.S.3    Huang, C.C.4    Ferrin, T.E.5
  • 34
    • 77952321234 scopus 로고    scopus 로고
    • The role of Cys108 in Trigonopsis variabilis Damino acid oxidase examined through chemical oxidation studies and point mutations C108S and C108D
    • doi:10.1016/j.bbapap.2010.02.009
    • Mueller M, Kratzer R, Schiller M, Slavica A, Rechberger G, Kollroser M, Nidetzky B (2010) The role of Cys108 in Trigonopsis variabilis Damino acid oxidase examined through chemical oxidation studies and point mutations C108S and C108D. BBA Proteins Proteom 1804(7):1483-1491. doi:10.1016/j.bbapap.2010.02. 009
    • (2010) BBA Proteins Proteom , vol.1804 , Issue.7 , pp. 1483-1491
    • Mueller, M.1    Kratzer, R.2    Schiller, M.3    Slavica, A.4    Rechberger, G.5    Kollroser, M.6    Nidetzky, B.7
  • 35
    • 84874081337 scopus 로고    scopus 로고
    • Diverse functional roles of reactive cysteines
    • doi:10.1021/cb3005269
    • Pace NJ, Weerapana E (2013) Diverse functional roles of reactive cysteines. ACS Chem Biol 8(2):283-296. doi:10.1021/cb3005269
    • (2013) ACS Chem Biol , vol.8 , Issue.2 , pp. 283-296
    • Pace, N.J.1    Weerapana, E.2
  • 36
    • 67849130559 scopus 로고    scopus 로고
    • HotSpot Wizard: A web server for identification of hot spots in protein engineering
    • doi:10.1093/nar/gkp410
    • Pavelka A, Chovancova E, Damborsky J (2009) HotSpot Wizard: a web server for identification of hot spots in protein engineering. Nucleic Acids Res 37(suppl 2):W376-W383. doi:10.1093/nar/gkp410
    • (2009) Nucleic Acids Res , vol.37 , Issue.SUPPL. 2
    • Pavelka, A.1    Chovancova, E.2    Damborsky, J.3
  • 37
    • 0036438892 scopus 로고    scopus 로고
    • Differential salt-induced stabilization of structure in the initial folding intermediate ensemble of barstar
    • DOI 10.1016/S0022-2836(02)01068-9
    • Pradeep L, Udgaonkar JB (2002) Differential salt-induced stabilization of structure in the initial folding intermediate ensemble of Barstar. J Mol Biol 324(2):331-347. doi:10.1016/S0022-2836(02)01068-9 (Pubitemid 35379032)
    • (2002) Journal of Molecular Biology , vol.324 , Issue.2 , pp. 331-347
    • Pradeep, L.1    Udgaonkar, J.B.2
  • 38
    • 0033572812 scopus 로고    scopus 로고
    • The role of cysteine residues in structure and enzyme activity of a maize beta-glucosidase
    • doi:10.1046/j.1432-1327.1999.00948.x
    • Rotrekl V, Nejedla E, Kucera I, Abdallah F, Palme K, Brzobohaty B (1999) The role of cysteine residues in structure and enzyme activity of a maize beta-glucosidase. Eur J Biochem/FEBS 266(3):1056-1065. doi:10.1046/j.1432-1327. 1999.00948.x
    • (1999) Eur J Biochem/FEBS , vol.266 , Issue.3 , pp. 1056-1065
    • Rotrekl, V.1    Nejedla, E.2    Kucera, I.3    Abdallah, F.4    Palme, K.5    Brzobohaty, B.6
  • 39
    • 76649127737 scopus 로고    scopus 로고
    • Thermococcus kodakarensis genetics: TK1827-encoded beta-glycosidase, new positive-selection protocol, and targeted and repetitive deletion technology
    • doi:10.1128/AEM.02497-09
    • Santangelo TJ, Cubonova L, Reeve JN (2010) Thermococcus kodakarensis genetics: TK1827-encoded beta-glycosidase, new positive-selection protocol, and targeted and repetitive deletion technology. Appl Environ Microb 76(4):1044-1052. doi:10.1128/AEM.02497-09
    • (2010) Appl Environ Microb , vol.76 , Issue.4 , pp. 1044-1052
    • Santangelo, T.J.1    Cubonova, L.2    Reeve, J.N.3
  • 40
    • 33745161382 scopus 로고    scopus 로고
    • Allosteric disulfide bonds
    • DOI 10.1021/bi0603064
    • Schmidt B, Ho L, Hogg PJ (2006) Allosteric disulfide bonds. Biochemistry 45(24):7429-7433. doi:10.1021/bi0603064 (Pubitemid 43894936)
    • (2006) Biochemistry , vol.45 , Issue.24 , pp. 7429-7433
    • Schmidt, B.1    Ho, L.2    Hogg, P.J.3
  • 41
    • 33745328074 scopus 로고    scopus 로고
    • The effect of engineered disulfide bonds on the stability of Drosophila melanogaster acetylcholinesterase
    • doi:10.1186/1471-2091-7-12
    • Siadat O, Lougarre A, Lamouroux L, Ladurantie C, Fournier D (2006) The effect of engineered disulfide bonds on the stability of Drosophila melanogaster acetylcholinesterase. BMC Biochem 7(1):12. doi:10.1186/1471-2091-7-12
    • (2006) BMC Biochem , vol.7 , Issue.1 , pp. 12
    • Siadat, O.1    Lougarre, A.2    Lamouroux, L.3    Ladurantie, C.4    Fournier, D.5
  • 42
    • 0021844602 scopus 로고
    • [beta]-Hairpin families in globular proteins
    • doi:10.1038/316170a0
    • Sibanda BL, Thornton JM (1985) [beta]-Hairpin families in globular proteins. Nature 316(6024):170 - 174. doi:10.1038/316170a0
    • (1985) Nature , vol.316 , Issue.6024 , pp. 170-174
    • Sibanda, B.L.1    Thornton, J.M.2
  • 43
    • 0036545550 scopus 로고    scopus 로고
    • Thermodynamic activation properties of elongation factor 2 (EF-2) proteins from psychrotolerant and thermophilic Archaea
    • DOI 10.1007/s007920100237
    • Siddiqui KS, Cavicchioli R, Thomas T (2002) Thermodynamic activation properties of elongation factor 2 (EF-2) proteins from psychrotolerant and thermophilic Archaea. Extremophiles 6(2):143-150. doi:10.1007/s007920100237 (Pubitemid 41490482)
    • (2002) Extremophiles , vol.6 , Issue.2 , pp. 143-150
    • Siddiqui, K.S.1    Cavicchioli, R.2    Thomas, T.3
  • 44
    • 24344448645 scopus 로고    scopus 로고
    • Role of disulfide bridges in the activity and stability of a cold-active alpha-amylase
    • DOI 10.1128/JB.187.17.6206-6212.2005
    • Siddiqui KS, Poljak A, Guilhaus M, Feller G, D'Amico S, Gerday C, Cavicchioli R (2005) Role of disulfide bridges in the activity and stability of a cold-active alpha-amylase. J Bacteriol 187(17):6206-6212. doi:10.1128/JB.187. 17.6206-6212.2005 (Pubitemid 41262817)
    • (2005) Journal of Bacteriology , vol.187 , Issue.17 , pp. 6206-6212
    • Siddiqui, K.S.1    Poljak, A.2    Guilhaus, M.3    Feller, G.4    D'Amico, S.5    Gerday, C.6    Cavicchioli, R.7
  • 46
    • 0029859281 scopus 로고    scopus 로고
    • Cloning and expression of the α-amylase gene from the hyperthermophilic archaeon Pyrococcus sp. KOD1, and characterization of the enzyme
    • doi:10.1016/0922-338X(96)88812-X
    • Tachibana Y, Leclere MM, Fujiwara S, Takagi M, Imanaka T (1996) Cloning and expression of the α-amylase gene from the hyperthermophilic archaeon Pyrococcus sp. KOD1, and characterization of the enzyme. J Ferment Bioeng 82(3):224-232. doi:10.1016/0922-338X(96)88812-X
    • (1996) J Ferment Bioeng , vol.82 , Issue.3 , pp. 224-232
    • Tachibana, Y.1    Leclere, M.M.2    Fujiwara, S.3    Takagi, M.4    Imanaka, T.5
  • 47
    • 78650356359 scopus 로고    scopus 로고
    • Inhibition of cellulase-catalyzed lignocellulosic hydrolysis by iron and oxidative metal ions and complexes
    • doi:10.1128/AEM.01376-10
    • Tejirian A, Xu F (2010) Inhibition of cellulase-catalyzed lignocellulosic hydrolysis by iron and oxidative metal ions and complexes. Appl Environ Microbiol 76(23):7673-7682. doi:10.1128/AEM.01376-10
    • (2010) Appl Environ Microbiol , vol.76 , Issue.23 , pp. 7673-7682
    • Tejirian, A.1    Xu, F.2
  • 48
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • DOI 10.1128/MMBR.65.1.1-43.2001
    • Vieille C, Zeikus GJ (2001) Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65(1):1-43. doi:10.1128/MMBR.65.1.1-43.2001 (Pubitemid 32204286)
    • (2001) Microbiology and Molecular Biology Reviews , vol.65 , Issue.1 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 49
    • 84879033533 scopus 로고    scopus 로고
    • Role of cysteine residues in thermal inactivation of fungal Cel6A cellobiohydrolases
    • doi:10.1016/j.bbapap.2013.05.003
    • Wu I, Heel T, Arnold FH (2013) Role of cysteine residues in thermal inactivation of fungal Cel6A cellobiohydrolases. BBA Proteins Proteom 1834(8):1539-1544. doi:10.1016/j.bbapap.2013.05.003
    • (2013) BBA Proteins Proteom , vol.1834 , Issue.8 , pp. 1539-1544
    • Wu, I.1    Heel, T.2    Arnold, F.H.3
  • 51
    • 80053442444 scopus 로고    scopus 로고
    • Disulfide bond formation and its impact on the biological activity and stability of recombinant therapeutic proteins produced by Escherichia coli expression system
    • doi:10.1016/j.biotechadv.2011.07.013
    • Zhang L, Chou CP, Moo-Young M (2011) Disulfide bond formation and its impact on the biological activity and stability of recombinant therapeutic proteins produced by Escherichia coli expression system. Biotechnol Adv 29(6):923-929. doi:10.1016/j.biotechadv.2011.07.013
    • (2011) Biotechnol Adv , vol.29 , Issue.6 , pp. 923-929
    • Zhang, L.1    Chou, C.P.2    Moo-Young, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.