메뉴 건너뛰기




Volumn 94, Issue 1, 2012, Pages 111-121

Rational design to improve thermostability and specific activity of the truncated Fibrobacter succinogenes 1,3-1,4-β-d-glucanase

Author keywords

Glucanase; Cellobiose; Cellotetraose; Crystal structure; Synchrotron radiation

Indexed keywords

CELLOBIOSE; CELLOTETRAOSE; CRUDE PROTEINS; DOUBLE MUTANTS; E. COLI; ENZYME STABILITY; FEED ADDITIVES; FIBROBACTER SUCCINOGENES; GLUCANASE; INDUSTRIAL FERMENTATION; P. PASTORIS; PICHIA PASTORIS; PLANT FIBERS; PROTEIN PRODUCTION; PROTEIN STABILITY; PROTEIN STRUCTURES; RATIONAL DESIGN; SIMILAR PATTERN; SINGLE MUTANT; SPECIFIC ACTIVITY; STRUCTURAL POINT; STRUCTURE-BASED; STRUCTURE-FUNCTION RELATIONSHIP; SUBSTRATE COMPLEXES; TURNOVER RATE; WILD-TYPE PROTEINS;

EID: 84858451153     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-011-3586-7     Document Type: Article
Times cited : (29)

References (29)
  • 1
    • 0028924376 scopus 로고
    • Purification of Thermotoga maritima enzymes for the degradation of cellulosic materials
    • 1:CAS:528:DyaK2MXksl2ls7c%3D
    • K Bronnenmeier A Kern W Liebl WL Staudenbauer 1995 Purification of Thermotoga maritima enzymes for the degradation of cellulosic materials Appl Environ Microbiol 61 4 1399 1407 1:CAS:528:DyaK2MXksl2ls7c%3D
    • (1995) Appl Environ Microbiol , vol.61 , Issue.4 , pp. 1399-1407
    • Bronnenmeier, K.1    Kern, A.2    Liebl, W.3    Staudenbauer, W.L.4
  • 2
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: The free R value. Methods and applications
    • 10.1107/S0907444992007352 10.1107/S0907444992007352 1:STN:280: DC%2BD2czpsVOmtQ%3D%3D
    • AT Brunger 1993 Assessment of phase accuracy by cross validation: the free R value. Methods and applications Acta Crystallogr D Biol Crystallogr 49 Pt 1 24 36 10.1107/S0907444992007352 10.1107/S0907444992007352 1:STN:280:DC%2BD2czpsVOmtQ%3D%3D
    • (1993) Acta Crystallogr D Biol Crystallogr , vol.49 , Issue.PART 1 , pp. 24-36
    • Brunger, A.T.1
  • 4
    • 0035947640 scopus 로고    scopus 로고
    • Directed mutagenesis of apecific active site residues on Fibrobacter succinogenes 1,3-1,4-beta-d-glucanase significantly affects catalysis and enzyme structural stability
    • 10.1074/jbc.M100843200 10.1074/jbc.M100843200 1:CAS:528: DC%2BD3MXktFWnu78%3D
    • JL Chen LC Tsai TN Wen JB Tang HS Yuan LF Shyur 2001 Directed mutagenesis of apecific active site residues on Fibrobacter succinogenes 1,3-1,4-beta-d-glucanase significantly affects catalysis and enzyme structural stability J Biol Chem 276 21 17895 17901 10.1074/jbc.M100843200 10.1074/jbc.M100843200 1:CAS:528:DC%2BD3MXktFWnu78%3D
    • (2001) J Biol Chem , vol.276 , Issue.21 , pp. 17895-17901
    • Chen, J.L.1    Tsai, L.C.2    Wen, T.N.3    Tang, J.B.4    Yuan, H.S.5    Shyur, L.F.6
  • 5
    • 77957938480 scopus 로고    scopus 로고
    • Structural and catalytic roles of amino acid residues located at substrate-binding pocket in Fibrobacter succinogenes 1,3-1,4-beta-d-glucanase
    • 10.1002/prot.22798 10.1002/prot.22798 1:CAS:528:DC%2BC3cXhtVGqs7zF
    • JH Chen LC Tsai HC Huang LF Shyur 2010 Structural and catalytic roles of amino acid residues located at substrate-binding pocket in Fibrobacter succinogenes 1,3-1,4-beta-d-glucanase Proteins 78 13 2820 2830 10.1002/prot.22798 10.1002/prot.22798 1:CAS:528:DC%2BC3cXhtVGqs7zF
    • (2010) Proteins , vol.78 , Issue.13 , pp. 2820-2830
    • Chen, J.H.1    Tsai, L.C.2    Huang, H.C.3    Shyur, L.F.4
  • 6
    • 0037047015 scopus 로고    scopus 로고
    • 203 residues on Fibrobacter succinogenes 1,3-1,4-β-D-glucanase significantly affects catalytic activities of the enzyme
    • DOI 10.1021/bi025766l
    • HL Cheng LC Tsai SS Lin HS Yuan NS Yang SH Lee LF Shyur 2002 Mutagenesis of Trp(54) and Trp(203) residues on Fibrobacter succinogenes 1,3-1,4-beta-d-glucanase significantly affects catalytic activities of the enzyme Biochemistry 41 27 8759 8766 bi025766l 10.1021/bi025766l 1:CAS:528:DC%2BD38Xktl2ntb0%3D (Pubitemid 34743317)
    • (2002) Biochemistry , vol.41 , Issue.27 , pp. 8759-8766
    • Cheng, H.-L.1    Tsai, L.-C.2    Lin, S.-S.3    Yuan, H.S.4    Yang, N.-S.5    Lee, S.-H.6    Shyur, L.-F.7
  • 7
    • 79952489592 scopus 로고    scopus 로고
    • Crystal structure and substrate-binding mode of cellulase 12A from Thermotoga maritima
    • 10.1002/prot.22953 10.1002/prot.22953 1:CAS:528:DC%2BC3MXkvVWrsbo%3D
    • YS Cheng TP Ko TH Wu Y Ma CH Huang HL Lai AH Wang JR Liu RT Guo 2011 Crystal structure and substrate-binding mode of cellulase 12A from Thermotoga maritima Proteins 79 4 1193 1204 10.1002/prot.22953 10.1002/prot.22953 1:CAS:528:DC%2BC3MXkvVWrsbo%3D
    • (2011) Proteins , vol.79 , Issue.4 , pp. 1193-1204
    • Cheng, Y.S.1    Ko, T.P.2    Wu, T.H.3    Ma, Y.4    Huang, C.H.5    Lai, H.L.6    Wang, A.H.7    Liu, J.R.8    Guo, R.T.9
  • 8
    • 0023684974 scopus 로고
    • Purification and properties of a 1,3-1,4-β-glucanase (lichenase, 1,3-1,4-β-D-glucan 4-glucanohydrolase, EC 3.2.1.73) from Bacteroides succinogenes cloned in Escherichia coli
    • JD Erfle RM Teather PJ Wood JE Irvin 1988 Purification and properties of a 1,3-1,4-beta-d-glucanase (lichenase, 1,3-1,4-beta-d-glucan 4-glucanohydrolase, EC 3.2.1.73) from Bacteroides succinogenes cloned in Escherichia coli Biochem J 255 3 833 841 1:CAS:528:DyaL1cXmt1Gnu7o%3D (Pubitemid 18263948)
    • (1988) Biochemical Journal , vol.255 , Issue.3 , pp. 833-841
    • Erfle, J.D.1    Teather, R.M.2    Wood, P.J.3    Irvin, J.E.4
  • 9
    • 0344289519 scopus 로고    scopus 로고
    • Role of glycosylation in the functional expression of an Aspergillus niger phytase (phyA) in Pichia pastoris
    • DOI 10.1006/abbi.1999.1115
    • Y Han XG Lei 1999 Role of glycosylation in the functional expression of an Aspergillus niger phytase (phyA) in Pichia pastoris Arch Biochem Biophys 364 1 83 90 S0003-9861(99)91115-3 10.1006/abbi.1999.1115 1:CAS:528: DyaK1MXhvFWisbY%3D (Pubitemid 29394294)
    • (1999) Archives of Biochemistry and Biophysics , vol.364 , Issue.1 , pp. 83-90
    • Han, Y.1    Lei, X.G.2
  • 10
    • 38349108789 scopus 로고    scopus 로고
    • High-level expression of a truncated 1,3-1,4-beta-d-glucanase from Fibrobacter succinogenes in Pichia pastoris by optimization of codons and fermentation
    • 10.1007/s00253-007-1290-4 10.1007/s00253-007-1290-4 1:CAS:528: DC%2BD1cXot1KmtQ%3D%3D
    • H Huang P Yang H Luo H Tang N Shao T Yuan Y Wang Y Bai B Yao 2008 High-level expression of a truncated 1,3-1,4-beta-d-glucanase from Fibrobacter succinogenes in Pichia pastoris by optimization of codons and fermentation Appl Microbiol Biotechnol 78 1 95 103 10.1007/s00253-007-1290-4 10.1007/s00253-007- 1290-4 1:CAS:528:DC%2BD1cXot1KmtQ%3D%3D
    • (2008) Appl Microbiol Biotechnol , vol.78 , Issue.1 , pp. 95-103
    • Huang, H.1    Yang, P.2    Luo, H.3    Tang, H.4    Shao, N.5    Yuan, T.6    Wang, Y.7    Bai, Y.8    Yao, B.9
  • 11
    • 33748569443 scopus 로고    scopus 로고
    • Mutational analysis of N-glycosylation recognition sites on the biochemical properties of Aspergillus kawachii α-l-arabinofuranosidase 54
    • DOI 10.1016/j.bbagen.2006.04.009, PII S0304416506001292
    • T Koseki Y Miwa Y Mese A Miyanaga S Fushinobu T Wakagi H Shoun H Matsuzawa K Hashizume 2006 Mutational analysis of N-glycosylation recognition sites on the biochemical properties of Aspergillus kawachii alpha-l- arabinofuranosidase 54 Biochim Biophys Acta 1760 9 1458 1464 S0304-4165(06)00129-2 10.1016/j.bbagen.2006.04.009 1:CAS:528: DC%2BD28Xps1CjsbY%3D (Pubitemid 44374212)
    • (2006) Biochimica et Biophysica Acta - General Subjects , vol.1760 , Issue.9 , pp. 1458-1464
    • Koseki, T.1    Miwa, Y.2    Mese, Y.3    Miyanaga, A.4    Fushinobu, S.5    Wakagi, T.6    Shoun, H.7    Matsuzawa, H.8    Hashizume, K.9
  • 12
    • 0029774346 scopus 로고    scopus 로고
    • Analysis of a Thermotoga maritima DNA fragment encoding two similar thermostable cellulases, CelA and CelB, and characterization of the recombinant enzymes
    • W Liebl P Ruile K Bronnenmeier K Riedel F Lottspeich I Greif 1996 Analysis of a Thermotoga maritima DNA fragment encoding two similar thermostable cellulases, CelA and CelB, and characterization of the recombinant enzymes Microbiology 142 Pt 9 2533 2542 10.1099/00221287-142-9-2533 1:CAS:528: DyaK28XlvF2gsLY%3D (Pubitemid 26333786)
    • (1996) Microbiology , vol.142 , Issue.9 , pp. 2533-2542
    • Liebl, W.1    Ruile, P.2    Bronnenmeier, K.3    Riedel, K.4    Lottspeich, F.5    Greif, I.6
  • 13
    • 61749100791 scopus 로고    scopus 로고
    • Structural and catalytic roles of residues located in beta13 strand and the following beta-turn loop in Fibrobacter succinogenes 1,3-1,4-beta-d- glucanase
    • 10.1016/j.bbagen.2009.01.013 1:CAS:528:DC%2BD1MXjt1ansrc%3D
    • YS Lin LC Tsai SH Lee HS Yuan LF Shyur 2009 Structural and catalytic roles of residues located in beta13 strand and the following beta-turn loop in Fibrobacter succinogenes 1,3-1,4-beta-d-glucanase Biochim Biophys Acta 1790 4 231 239 10.1016/j.bbagen.2009.01.013 1:CAS:528:DC%2BD1MXjt1ansrc%3D
    • (2009) Biochim Biophys Acta , vol.1790 , Issue.4 , pp. 231-239
    • Lin, Y.S.1    Tsai, L.C.2    Lee, S.H.3    Yuan, H.S.4    Shyur, L.F.5
  • 14
    • 70350455262 scopus 로고    scopus 로고
    • The prospects of cellulase-producing bacteria for the bioconversion of lignocellulosic biomass
    • 10.7150/ijbs.5.500 1:CAS:528:DC%2BD1MXhtVemtbzM
    • M Maki KT Leung W Qin 2009 The prospects of cellulase-producing bacteria for the bioconversion of lignocellulosic biomass Int J Biol Sci 5 5 500 516 10.7150/ijbs.5.500 1:CAS:528:DC%2BD1MXhtVemtbzM
    • (2009) Int J Biol Sci , vol.5 , Issue.5 , pp. 500-516
    • Maki, M.1    Leung, K.T.2    Qin, W.3
  • 15
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • DOI 10.1006/jsbi.1999.4094
    • DE McRee 1999 XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density J Struct Biol 125 2-3 156 165 S1047-8477(99)94094-7 10.1006/jsbi.1999.4094 1:CAS:528:DyaK1MXis1Krt7k%3D (Pubitemid 29402600)
    • (1999) Journal of Structural Biology , vol.125 , Issue.2-3 , pp. 156-165
    • McRee, D.E.1
  • 16
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • 10.1021/ac60147a030 1:CAS:528:DyaG1MXmtFKiuw%3D%3D
    • GL Miller 1959 Use of dinitrosalicylic acid reagent for determination of reducing sugar Anal Chem 31 3 426 428 10.1021/ac60147a030 1:CAS:528: DyaG1MXmtFKiuw%3D%3D
    • (1959) Anal Chem , vol.31 , Issue.3 , pp. 426-428
    • Miller, G.L.1
  • 18
    • 0034731485 scopus 로고    scopus 로고
    • Bacterial 1,3-1,4-beta-glucanases: Structure, function and protein engineering
    • S0167-4838(00)00231-4 10.1016/S0167-4838(00)00231-4 1:CAS:528: DC%2BD3MXitl2ksg%3D%3D
    • A Planas 2000 Bacterial 1,3-1,4-beta-glucanases: structure, function and protein engineering Biochim Biophys Acta 1543 2 361 382 S0167-4838(00)00231-4 10.1016/S0167-4838(00)00231-4 1:CAS:528:DC%2BD3MXitl2ksg%3D%3D
    • (2000) Biochim Biophys Acta , vol.1543 , Issue.2 , pp. 361-382
    • Planas, A.1
  • 19
    • 0030269964 scopus 로고    scopus 로고
    • The rumen: A unique source of enzymes for enhancing livestock production
    • DOI 10.1006/anae.1996.0036
    • LB Selinger CW Forsberg KJ Cheng 1996 The rumen: a unique source of enzymes for enhancing livestock production Anaerobe 2 5 263 284 S1075-9964(96)90036-0 10.1006/anae.1996.0036 1:CAS:528:DyaK2sXisFOhug%3D%3D (Pubitemid 26421337)
    • (1996) Anaerobe , vol.2 , Issue.5 , pp. 263-284
    • Selinger, L.B.1    Forsberg, C.W.2    Cheng, K.-J.3
  • 20
    • 0036231497 scopus 로고    scopus 로고
    • Production of glycosylated thermostable Providencia rettgeri penicillin G amidase in Pichia pastoris
    • DOI 10.1016/S1567-1356(01)00040-X, PII S156713560100040X
    • M Sevo G Degrassi N Skoko V Venturi G Ljubijankic 2002 Production of glycosylated thermostable Providencia rettgeri penicillin G amidase in Pichia pastoris FEMS Yeast Res 1 4 271 277 S156713560100040X 1:CAS:528: DC%2BD38XivVyrurg%3D (Pubitemid 34442255)
    • (2002) FEMS Yeast Research , vol.1 , Issue.4 , pp. 271-277
    • Sevo, M.1    Degrassi, G.2    Skoko, N.3    Venturi, V.4    Ljubijankic, G.5
  • 22
    • 0034831370 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of the 1,3-1,4-β-D-glucanase from Fibrobacter succinogenes
    • DOI 10.1107/S0907444901010381
    • LC Tsai LF Shyur SS Lin HS Yuan 2001 Crystallization and preliminary X-ray diffraction analysis of the 1,3-1,4-beta-d-glucanase from Fibrobacter succinogenes Acta Crystallogr D Biol Crystallogr 57 Pt 9 1303 1306 S0907444901010381 10.1107/S0907444901010381 1:STN:280:DC%2BD3Mvot1GqsQ%3D%3D (Pubitemid 32885731)
    • (2001) Acta Crystallographica Section D: Biological Crystallography , vol.57 , Issue.9 , pp. 1303-1306
    • Tsai, L.-C.1    Shyur, L.-F.2    Lin, S.-S.3    Yuan, H.S.4
  • 23
    • 0038723696 scopus 로고    scopus 로고
    • Crystal structure of a natural circularly permuted jellyroll protein: 1,3-1,4-β-D-glucanase from Fibrobacter succinogenes
    • DOI 10.1016/S0022-2836(03)00630-2
    • LC Tsai LF Shyur SH Lee SS Lin HS Yuan 2003 Crystal structure of a natural circularly permuted jellyroll protein: 1,3-1,4-beta-d-glucanase from Fibrobacter succinogenes J Mol Biol 330 3 607 620 S0022283603006302 10.1016/S0022-2836(03)00630-2 1:CAS:528:DC%2BD3sXkvFGgt78%3D (Pubitemid 36808691)
    • (2003) Journal of Molecular Biology , vol.330 , Issue.3 , pp. 607-620
    • Tsai, L.-C.1    Shyur, L.-F.2    Lee, S.-H.3    Lin, S.-S.4    Yuan, H.S.5
  • 24
    • 27744535276 scopus 로고    scopus 로고
    • Crystal structure of truncated Fibrobacter succinogenes 1,3-1,4-β-D-glucanase in complex with β-1,3-1,4-cellotriose
    • DOI 10.1016/j.jmb.2005.09.041, PII S0022283605011071
    • LC Tsai LF Shyur YS Cheng SH Lee 2005 Crystal structure of truncated Fibrobacter succinogenes 1,3-1,4-beta-d-glucanase in complex with beta-1,3-1,4-cellotriose J Mol Biol 354 3 642 651 S0022-2836(05)01107-1 10.1016/j.jmb.2005.09.041 1:CAS:528:DC%2BD2MXht1ejsrzF (Pubitemid 41628282)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.3 , pp. 642-651
    • Tsai, L.-C.1    Shyur, L.-F.2    Cheng, Y.-S.3    Lee, S.-H.4
  • 25
    • 56049086111 scopus 로고    scopus 로고
    • Structural modeling of glucanase-substrate complexes suggests a conserved tyrosine is involved in carbohydrate recognition in plant 1,3-1,4-beta-d- glucanases
    • 10.1007/s10822-008-9228-1 10.1007/s10822-008-9228-1 1:CAS:528: DC%2BD1cXhtlags7bO
    • LC Tsai YN Chen LF Shyur 2008 Structural modeling of glucanase-substrate complexes suggests a conserved tyrosine is involved in carbohydrate recognition in plant 1,3-1,4-beta-d-glucanases J Comput Aided Mol Des 22 12 915 923 10.1007/s10822-008-9228-1 10.1007/s10822-008-9228-1 1:CAS:528:DC%2BD1cXhtlags7bO
    • (2008) J Comput Aided Mol des , vol.22 , Issue.12 , pp. 915-923
    • Tsai, L.C.1    Chen, Y.N.2    Shyur, L.F.3
  • 26
    • 56649117571 scopus 로고    scopus 로고
    • Mutational and structural studies of the active-site residues in truncated Fibrobacter succinogenes 1,3-1,4-beta-d-glucanase
    • S0907444908033428 10.1107/S0907444908033428
    • LC Tsai HC Huang CH Hsiao YN Chiang LF Shyur YS Lin SH Lee 2008 Mutational and structural studies of the active-site residues in truncated Fibrobacter succinogenes 1,3-1,4-beta-d-glucanase Acta Crystallogr D Biol Crystallogr 64 Pt 12 1259 1266 S0907444908033428 10.1107/S0907444908033428
    • (2008) Acta Crystallogr D Biol Crystallogr , vol.64 , Issue.PART 12 , pp. 1259-1266
    • Tsai, L.C.1    Huang, H.C.2    Hsiao, C.H.3    Chiang, Y.N.4    Shyur, L.F.5    Lin, Y.S.6    Lee, S.H.7
  • 27
    • 0036669448 scopus 로고    scopus 로고
    • Selection of mutations for increased protein stability
    • DOI 10.1016/S0958-1669(02)00325-7
    • B van den Burg VG Eijsink 2002 Selection of mutations for increased protein stability Curr Opin Biotechnol 13 4 333 337 S0958166902003257 10.1016/S0958-1669(02)00325-7 (Pubitemid 35254091)
    • (2002) Current Opinion in Biotechnology , vol.13 , Issue.4 , pp. 333-337
    • Van Den Burg, B.1    Eijsink, V.G.2
  • 28
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • DOI 10.1128/MMBR.65.1.1-43.2001
    • C Vieille GJ Zeikus 2001 Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability Microbiol Mol Biol Rev 65 1 1 43 10.1128/MMBR.65.1.1-43.2001 10.1128/MMBR.65.1.1-43.2001 1:CAS:528: DC%2BD3MXisFyms74%3D (Pubitemid 32204286)
    • (2001) Microbiology and Molecular Biology Reviews , vol.65 , Issue.1 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 29
    • 21744452510 scopus 로고    scopus 로고
    • A truncated Fibrobacter succinogenes 1,3-1,4-β-D-glucanase with improved enzymatic activity and thermotolerance
    • DOI 10.1021/bi0500630
    • TN Wen JL Chen SH Lee NS Yang LF Shyur 2005 A truncated Fibrobacter succinogenes 1,3-1,4-beta-d-glucanase with improved enzymatic activity and thermotolerance Biochemistry 44 25 9197 9205 10.1021/bi0500630 10.1021/bi0500630 1:CAS:528:DC%2BD2MXks1Sntrc%3D (Pubitemid 40943234)
    • (2005) Biochemistry , vol.44 , Issue.25 , pp. 9197-9205
    • Wen, T.-N.1    Chen, J.-L.2    Lee, S.-H.3    Yang, N.-S.4    Shyur, L.-F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.