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Volumn 1790, Issue 4, 2009, Pages 231-239

Structural and catalytic roles of residues located in β13 strand and the following β-turn loop in Fibrobacter succinogenes 1,3-1,4-β-d-glucanase

Author keywords

1,3 1,4 d glucanase; Catalytic efficiency; Comparative energy Gb; Fibrobacter succinogenes; Structural modeling

Indexed keywords

AMINO ACID; BETA GLUCAN HYDROLASE; FIBROBACTER SUCCINOGENES 1,3 1,4 BETA DEXTRO GLUCANASE; UNCLASSIFIED DRUG;

EID: 61749100791     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2009.01.013     Document Type: Article
Times cited : (5)

References (34)
  • 1
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies G., and Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 3 (1995) 853-859
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 2
    • 0016611070 scopus 로고
    • A new substrate for investigating the specificity of β-glucan hydrolases
    • Anderson M.A., and Stone B.A. A new substrate for investigating the specificity of β-glucan hydrolases. FEBS Lett. 51 (1975) 202-207
    • (1975) FEBS Lett. , vol.51 , pp. 202-207
    • Anderson, M.A.1    Stone, B.A.2
  • 3
    • 0001449372 scopus 로고
    • Water-soluble (1 → 3),(1 → 4)-β-d-glucans from barley (Hordeum vulgare) endosperm. II. Fine structure
    • Woodward J.R., Fincher G.B., and Stone B.A. Water-soluble (1 → 3),(1 → 4)-β-d-glucans from barley (Hordeum vulgare) endosperm. II. Fine structure. Carbohydr. Polym. 3 (1983) 207-225
    • (1983) Carbohydr. Polym. , vol.3 , pp. 207-225
    • Woodward, J.R.1    Fincher, G.B.2    Stone, B.A.3
  • 4
    • 0034731485 scopus 로고    scopus 로고
    • Bacterial 1,3-1,4-β-glucanases: structure, function and protein engineering
    • Planas A. Bacterial 1,3-1,4-β-glucanases: structure, function and protein engineering. Biochim. Biophys. Acta 1543 (2000) 361-382
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 361-382
    • Planas, A.1
  • 5
    • 0021760542 scopus 로고
    • The DNA sequence of the gene and genetic control sites for the excreted B. subtilis enzyme β-glucanase
    • Murphy N., McConnell D.J., and Cantwell B.A. The DNA sequence of the gene and genetic control sites for the excreted B. subtilis enzyme β-glucanase. Nucleic Acids Res. 12 (1984) 5355-5367
    • (1984) Nucleic Acids Res. , vol.12 , pp. 5355-5367
    • Murphy, N.1    McConnell, D.J.2    Cantwell, B.A.3
  • 6
    • 0021238565 scopus 로고
    • Cloning and expression of a Bacillus subtilis endo-1,3-1,4-β-d-glucanase gene in Escherichia coli K12
    • Hinchliffe E. Cloning and expression of a Bacillus subtilis endo-1,3-1,4-β-d-glucanase gene in Escherichia coli K12. J. Gen. Microbiol. 130 (1984) 1285-1291
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 1285-1291
    • Hinchliffe, E.1
  • 7
    • 0027475578 scopus 로고
    • Characterization, cloning and sequencing of a thermostable endo-(1,3-1,4) β-glucanase-encoding gene from an alkalophilic Bacillus brevis
    • Louw M.E., Reid S.J., and Watson T.G. Characterization, cloning and sequencing of a thermostable endo-(1,3-1,4) β-glucanase-encoding gene from an alkalophilic Bacillus brevis. Appl. Microbiol. Biotechnol. 38 (1993) 507-513
    • (1993) Appl. Microbiol. Biotechnol. , vol.38 , pp. 507-513
    • Louw, M.E.1    Reid, S.J.2    Watson, T.G.3
  • 8
    • 0025335454 scopus 로고
    • Structure of the beta-1,3-1,4-glucanase gene of Bacillus macerans: homologies to other beta-glucanases
    • Borriss R., Buettner K., and Maentsaelae P. Structure of the beta-1,3-1,4-glucanase gene of Bacillus macerans: homologies to other beta-glucanases. Mol. Gen. Genet. 222 (1990) 278-283
    • (1990) Mol. Gen. Genet. , vol.222 , pp. 278-283
    • Borriss, R.1    Buettner, K.2    Maentsaelae, P.3
  • 9
    • 0022919704 scopus 로고
    • The β-glucanase gene from Bacillus amyloliquefaciens shows extensive homology with that of Bacillus subtilis
    • Hofemeister J., Kurtz A., Borriss R., and Knowles J. The β-glucanase gene from Bacillus amyloliquefaciens shows extensive homology with that of Bacillus subtilis. Gene 49 (1986) 177-187
    • (1986) Gene , vol.49 , pp. 177-187
    • Hofemeister, J.1    Kurtz, A.2    Borriss, R.3    Knowles, J.4
  • 10
    • 0025819512 scopus 로고
    • Molecular cloning, expression and nucleotide sequence of the endo-β-1,3-1,4-d-glucanase gene from Bacillus licheniformis. Predictive structural analyses of the encoded polypeptide
    • Lloberas J., Perez-Pons J.A., and Querol E. Molecular cloning, expression and nucleotide sequence of the endo-β-1,3-1,4-d-glucanase gene from Bacillus licheniformis. Predictive structural analyses of the encoded polypeptide. Eur. J. Biochem. 197 (1991) 337-343
    • (1991) Eur. J. Biochem. , vol.197 , pp. 337-343
    • Lloberas, J.1    Perez-Pons, J.A.2    Querol, E.3
  • 11
    • 0025366083 scopus 로고
    • DNA sequence of a Fibrobacter succinogenes mixed-linkage β-glucanase (1,3-1,4-β-d-glucan 4-glucanohydrolase) gene
    • Teather R.M., and Erfle J.D. DNA sequence of a Fibrobacter succinogenes mixed-linkage β-glucanase (1,3-1,4-β-d-glucan 4-glucanohydrolase) gene. J. Bacteriol. 172 (1990) 3837-3841
    • (1990) J. Bacteriol. , vol.172 , pp. 3837-3841
    • Teather, R.M.1    Erfle, J.D.2
  • 12
    • 0027231373 scopus 로고
    • A bifunctional enzyme, with separate xylanase and β(1,3-1,4)-glucanase domains, encoded by the xynD gene of Ruminococcus flavefaciens
    • Flint H.J., Martin J., McPherson C.A., Daniel A.S., and Zhang J.X. A bifunctional enzyme, with separate xylanase and β(1,3-1,4)-glucanase domains, encoded by the xynD gene of Ruminococcus flavefaciens. J. Bacteriol. 175 (1993) 2943-2951
    • (1993) J. Bacteriol. , vol.175 , pp. 2943-2951
    • Flint, H.J.1    Martin, J.2    McPherson, C.A.3    Daniel, A.S.4    Zhang, J.X.5
  • 13
    • 0025772933 scopus 로고
    • Properties of a thermoactive β-1,3-1,4-glucanase (lichenase) from Clostridium thermocellum expressed in Escherichia coli
    • Schimming S., Schwarz W.H., and Staudenbauer W.L. Properties of a thermoactive β-1,3-1,4-glucanase (lichenase) from Clostridium thermocellum expressed in Escherichia coli. Biochem. Biophys. Res. Commun. 177 (1991) 447-452
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 447-452
    • Schimming, S.1    Schwarz, W.H.2    Staudenbauer, W.L.3
  • 18
    • 0001204416 scopus 로고
    • Viscosity of beta-d-glucan as a factor in the enzymatic improvement of barley for chicks
    • White W.B., Bird H.R., Sunde M.L., and Marlett J.A. Viscosity of beta-d-glucan as a factor in the enzymatic improvement of barley for chicks. Poult. Sci. 62 (1983) 853-862
    • (1983) Poult. Sci. , vol.62 , pp. 853-862
    • White, W.B.1    Bird, H.R.2    Sunde, M.L.3    Marlett, J.A.4
  • 19
    • 0026569381 scopus 로고
    • Structure of the Clostridium thermocellum gene-licB and the encoded β-l,3-1,4-glucanase - a catalytic region homologous to Bacillus lichenases joined to the reiterated domain of clostridial cellulases
    • Schimming S., Schwarz W.H., and Staudenbauer W.L. Structure of the Clostridium thermocellum gene-licB and the encoded β-l,3-1,4-glucanase - a catalytic region homologous to Bacillus lichenases joined to the reiterated domain of clostridial cellulases. Eur. J. Biochem. 204 (1992) 13-19
    • (1992) Eur. J. Biochem. , vol.204 , pp. 13-19
    • Schimming, S.1    Schwarz, W.H.2    Staudenbauer, W.L.3
  • 20
    • 0029360566 scopus 로고
    • Circular permutations of protein sequence: not so rare?
    • Heinemann U., and Hahn M. Circular permutations of protein sequence: not so rare?. Trends Biochem. Sci. 20 (1995) 349-350
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 349-350
    • Heinemann, U.1    Hahn, M.2
  • 21
    • 0038723696 scopus 로고    scopus 로고
    • Crystal structure of a natural circularly permuted jellyroll protein: 1,3-1,4-β-d-glucanase from Fibrobacter succinogenes
    • Tsai L.-C., Shyur L.-F., Lee S.-H., Lin S.-S., and Yuan H.-S. Crystal structure of a natural circularly permuted jellyroll protein: 1,3-1,4-β-d-glucanase from Fibrobacter succinogenes. J. Mol. Biol. 330 (2003) 607-620
    • (2003) J. Mol. Biol. , vol.330 , pp. 607-620
    • Tsai, L.-C.1    Shyur, L.-F.2    Lee, S.-H.3    Lin, S.-S.4    Yuan, H.-S.5
  • 22
    • 21744452510 scopus 로고    scopus 로고
    • A truncated Fibrobacter succinogenes 1,3-1,4-β-d-glucanase with improved enzymatic activity and thermotolerance
    • Wen T.-N., Chen J.-L., Lee S.-H., Yang N.-S., and Shyur L.-F. A truncated Fibrobacter succinogenes 1,3-1,4-β-d-glucanase with improved enzymatic activity and thermotolerance. Biochemistry 44 (2005) 9197-9205
    • (2005) Biochemistry , vol.44 , pp. 9197-9205
    • Wen, T.-N.1    Chen, J.-L.2    Lee, S.-H.3    Yang, N.-S.4    Shyur, L.-F.5
  • 23
    • 0035947640 scopus 로고    scopus 로고
    • Directed mutagenesis of specific active site residues on Fibrobacter succinogenes 1,3-1,4-β-d-glucanase significantly affects catalysis and enzyme structural stability
    • Chen J.-L., Tsai L.-J., Wen T.-N., Tang J.-B., Yuan H.-S., and Shyur L.-F. Directed mutagenesis of specific active site residues on Fibrobacter succinogenes 1,3-1,4-β-d-glucanase significantly affects catalysis and enzyme structural stability. J. Biol. Chem. 276 (2001) 17895-17901
    • (2001) J. Biol. Chem. , vol.276 , pp. 17895-17901
    • Chen, J.-L.1    Tsai, L.-J.2    Wen, T.-N.3    Tang, J.-B.4    Yuan, H.-S.5    Shyur, L.-F.6
  • 25
    • 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
    • Tsai L.-C., Shyur L.-F., Cheng Y.-S., and Lee S.-H. Crystal structure of truncated Fibrobacter succinogenes 1,3-1,4-β-d-glucanase in complex with β-1,3-1,4-cellotriose. J. Mol. Biol. 354 (2005) 642-651
    • (2005) J. Mol. Biol. , vol.354 , pp. 642-651
    • Tsai, L.-C.1    Shyur, L.-F.2    Cheng, Y.-S.3    Lee, S.-H.4
  • 26
    • 0028841188 scopus 로고
    • Crystal structure of Bacillus licheniformis 1,3-1,4-β-d-glucan 4-glucanohydrolase at 1.8 Å resolution
    • Hahn M., Pons J., Planas A., Querol E., and Heinemann U. Crystal structure of Bacillus licheniformis 1,3-1,4-β-d-glucan 4-glucanohydrolase at 1.8 Å resolution. FEBS Lett. 374 (1995) 221-224
    • (1995) FEBS Lett. , vol.374 , pp. 221-224
    • Hahn, M.1    Pons, J.2    Planas, A.3    Querol, E.4    Heinemann, U.5
  • 27
    • 0030949353 scopus 로고    scopus 로고
    • Mutational analysis of the major loop of Bacillus 1,3-1,4-β-d-glucan 4-glucanohydrolases
    • Pons J., Querol E., and Planas A. Mutational analysis of the major loop of Bacillus 1,3-1,4-β-d-glucan 4-glucanohydrolases. J. Biol. Chem. 272 (1997) 13006-13012
    • (1997) J. Biol. Chem. , vol.272 , pp. 13006-13012
    • Pons, J.1    Querol, E.2    Planas, A.3
  • 28
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31 (1959) 426-428
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 29
    • 0002908272 scopus 로고
    • The TURBO-FRODO graphics package
    • Silicon Graphics, Mountain View, CA
    • Roussel A., and Cambillau C. The TURBO-FRODO graphics package. Graphics Geometry Partners Directory Vol. 81 (1992), Silicon Graphics, Mountain View, CA
    • (1992) Graphics Geometry Partners Directory , vol.81
    • Roussel, A.1    Cambillau, C.2
  • 30
    • 0021107943 scopus 로고
    • Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation
    • Wilkinson A.J., Fersht A.R., Blow D.M., and Winter G. Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation. Biochemistry 22 (1983) 3581-3586
    • (1983) Biochemistry , vol.22 , pp. 3581-3586
    • Wilkinson, A.J.1    Fersht, A.R.2    Blow, D.M.3    Winter, G.4
  • 34
    • 0027412196 scopus 로고
    • ALSCRIPT-A tool to format multiple sequence alignments
    • Barton G.J. ALSCRIPT-A tool to format multiple sequence alignments. Protein Eng. 6 (1993) 37-40
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.