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Volumn 370, Issue 3, 2003, Pages 793-804

Sphingomonas paucimobilis β-glucosidase Bgl1: A member of a new bacterial subfamily in glycoside hydrolase family 1

Author keywords

glucosidase; bgl1 gene; CAZy database; Hydrolase family 1; Periplasmic proteins; Sphingomonas paucimobilis

Indexed keywords

AMINO ACIDS; BACTERIA; BIOLOGICAL MEMBRANES; CELLULOSE; ESCHERICHIA COLI; GENETIC ENGINEERING; HYDROLYSIS;

EID: 0037444765     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021249     Document Type: Article
Times cited : (45)

References (54)
  • 1
    • 11944256494 scopus 로고
    • Catalytic mechanisms of glycosyl transfer
    • Sinnott, M. L. (1990) Catalytic mechanisms of glycosyl transfer. Chem. Rev. 90, 1171-1202
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 2
    • 0033963529 scopus 로고    scopus 로고
    • Glycosidase mechanisms: Anatomy of a finely tuned catalyst
    • Zechel, D. and Withers, S. J. (2000) Glycosidase mechanisms: anatomy of a finely tuned catalyst. Acc. Chem. Res. 33, 11-18
    • (2000) Acc. Chem. Res. , vol.33 , pp. 11-18
    • Zechel, D.1    Withers, S.J.2
  • 3
    • 0035348187 scopus 로고    scopus 로고
    • The celA gene, encoding a glycosyl hydrolase family 3 β-glucosidase in Azospirillum irakense, is required for optimal growth on cellobiosides
    • Faure, D., Henrissat, B., Ptacek, D., Bekri, M. A. and Vanderleyden, J. (2001) The celA gene, encoding a glycosyl hydrolase family 3 β-glucosidase in Azospirillum irakense, is required for optimal growth on cellobiosides. Appl. Environ. Microbiol. 67, 2380-2383
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2380-2383
    • Faure, D.1    Henrissat, B.2    Ptacek, D.3    Bekri, M.A.4    Vanderleyden, J.5
  • 4
    • 0025168749 scopus 로고
    • Molecular biology of cellulose degradation
    • Beguin, P. (1990) Molecular biology of cellulose degradation. Annu. Rev. Microbiol. 44, 219-248
    • (1990) Annu. Rev. Microbiol. , vol.44 , pp. 219-248
    • Beguin, P.1
  • 5
    • 0026718709 scopus 로고
    • A molecular and biochemical analysis of the structure of the cyanogenic β-glucosidase (linamarase) from cassava (Manihot esculenta Cranz)
    • Hughes, M. A., Brown, K., Pancoro, A., Murray, B. S., Oxtoby, E. and Hughes, J. (1992) A molecular and biochemical analysis of the structure of the cyanogenic β-glucosidase (linamarase) from cassava (Manihot esculenta Cranz). Arch. Biochem. Biophys. 295, 273-279
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 273-279
    • Hughes, M.A.1    Brown, K.2    Pancoro, A.3    Murray, B.S.4    Oxtoby, E.5    Hughes, J.6
  • 6
    • 0026055308 scopus 로고
    • Classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. (1991) Classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280, 309-316
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 7
    • 0029554594 scopus 로고
    • β-Glucosidase families revealed by computer analysis of protein sequences
    • Rojas, A., Arola, L. and Romeu, A. (1995) β-Glucosidase families revealed by computer analysis of protein sequences. Biochem. Mol. Biol. Int. 35, 1223-1231
    • (1995) Biochem. Mol. Biol. Int. , vol.35 , pp. 1223-1231
    • Rojas, A.1    Arola, L.2    Romeu, A.3
  • 8
    • 0001849438 scopus 로고    scopus 로고
    • The modular structure of cellulases and other carbohydrate-active enzymes: An integrated database approach
    • Ohmiya, K., Hayashi, K., Sakka, K., Kobayashi, Y., Karita, S. and Kimura, T., eds., Uni Publishers Co., Tokyo
    • Coutinho, P. and Henrissat, B. (1999) The modular structure of cellulases and other carbohydrate-active enzymes: an integrated database approach. In Genetics, Biochemistry and Ecology of Cellulose Degradation (Ohmiya, K., Hayashi, K., Sakka, K., Kobayashi, Y., Karita, S. and Kimura, T., eds.), pp. 15-23, Uni Publishers Co., Tokyo
    • (1999) Genetics, Biochemistry and Ecology of Cellulose Degradation , pp. 15-23
    • Coutinho, P.1    Henrissat, B.2
  • 9
    • 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, J. P. and 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, 7090-7094
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.P.5    Davies, G.6
  • 10
    • 0012854931 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 11
    • 0034671719 scopus 로고    scopus 로고
    • High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base
    • Burmeister, W. P., Cottaz, S., Rollin, P., Vasella, A. and Henrissat, B. (2000) High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base. J. Biol. Chem. 275, 39385-39393
    • (2000) J. Biol. Chem. , vol.275 , pp. 39385-39393
    • Burmeister, W.P.1    Cottaz, S.2    Rollin, P.3    Vasella, A.4    Henrissat, B.5
  • 12
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies, G. J., Wilson, K. S. and Henrissat, B. (1997) Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem J. 321, 557-559
    • (1997) Biochem. J. , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 13
    • 0034610330 scopus 로고    scopus 로고
    • The mechanism of substrate (aglycone) specificity in β-glucosidases is revealed by crystal structures of mutant maize β-glucosidase-DIMBOA, -DIMBOAGIc, and -dhurrin complexes
    • Czjzek, M., Cicek, M., Zamboni, V., Bevan, D. R., Henrissat, B. and Esen, A. (2000) The mechanism of substrate (aglycone) specificity in β-glucosidases is revealed by crystal structures of mutant maize β-glucosidase-DIMBOA, -DIMBOAGIc, and -dhurrin complexes. Proc. Natl. Acad. Sci. U.S.A. 97, 13555-13560
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13555-13560
    • Czjzek, M.1    Cicek, M.2    Zamboni, V.3    Bevan, D.R.4    Henrissat, B.5    Esen, A.6
  • 14
    • 0035865504 scopus 로고    scopus 로고
    • Crystal structure of a monocotyledon (maize ZMGlu1) β-glucosidase and a model of its complex with p-nitrophenyl β-D-thioglucoside
    • Czjzek, M., Cicek, M., Zamboni, V., Burmeister, W. P., Bevan, D. R., Henrissat, B. and Esen, A. (2001) Crystal structure of a monocotyledon (maize ZMGlu1) β-glucosidase and a model of its complex with p-nitrophenyl β-D-thioglucoside. Biochem. J. 354, 37-46
    • (2001) Biochem. J. , vol.354 , pp. 37-46
    • Czjzek, M.1    Cicek, M.2    Zamboni, V.3    Burmeister, W.P.4    Bevan, D.R.5    Henrissat, B.6    Esen, A.7
  • 15
    • 0019952782 scopus 로고
    • Agar-like polysaccharide produced by a Pseudomonas species: Production and basic properties
    • Kang, K. S., Veeder, G. T., Mirrasoul, P. J., Kaneko, T. and Cottrell, W. (1982) Agar-like polysaccharide produced by a Pseudomonas species: production and basic properties. Appl. Environ. Microbiol. 43, 1086-1091
    • (1982) Appl. Environ. Microbiol. , vol.43 , pp. 1086-1091
    • Kang, K.S.1    Veeder, G.T.2    Mirrasoul, P.J.3    Kaneko, T.4    Cottrell, W.5
  • 16
    • 0028917702 scopus 로고
    • Taxonimic study of bacteria isolated from plants: Proposal of Sphingomonas rosa sp. nov. Sphingomonas pruni sp. nov., and Sphingomonas mali sp. nov.
    • Takeuchi, M., Sakane, T., Yanagi, M., Yamasato, K., Hamana, K. and Yokota, A. (1995) Taxonimic study of bacteria isolated from plants: proposal of Sphingomonas rosa sp. nov., Sphingomonas pruni sp. nov., and Sphingomonas mali sp. nov. Int. J. Syst. Bacteriol. 45, 334-341
    • (1995) Int. J. Syst. Bacteriol. , vol.45 , pp. 334-341
    • Takeuchi, M.1    Sakane, T.2    Yanagi, M.3    Yamasato, K.4    Hamana, K.5    Yokota, A.6
  • 18
    • 0034066101 scopus 로고    scopus 로고
    • Chemotaxanomic and phylogenetic analyses of Sphingomonas strains isolated from ears of plants in the family Gramineae and a proposal of Sphingomonas roseoflava sp. nov.
    • Yun, N. R., Shin, Y. K., Hwang, S. Y., Kuraishi, H., Sugiyama, J. and Kawahara, K. (2000) Chemotaxanomic and phylogenetic analyses of Sphingomonas strains isolated from ears of plants in the family Gramineae and a proposal of Sphingomonas roseoflava sp. nov. J. Gen. Appl. Microbiol. 46, 9-18
    • (2000) J. Gen. Appl. Microbiol. , vol.46 , pp. 9-18
    • Yun, N.R.1    Shin, Y.K.2    Hwang, S.Y.3    Kuraishi, H.4    Sugiyama, J.5    Kawahara, K.6
  • 19
    • 0034016761 scopus 로고    scopus 로고
    • Identification of pgmG gene, encoding a bifunctional protein with phosphoglucomutase and phosphomannomutase activities, in gellan gum producing strain Sphingomonas paucimobilis ATCC 31461
    • Videira, P. A., Cortes, L. L., Fialho, A. M. and Sá-Correia, I. (2000) Identification of pgmG gene, encoding a bifunctional protein with phosphoglucomutase and phosphomannomutase activities, in gellan gum producing strain Sphingomonas paucimobilis ATCC 31461. Appl. Environ. Microbiol. 66, 2252-2258
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2252-2258
    • Videira, P.A.1    Cortes, L.L.2    Fialho, A.M.3    Sá-Correia, I.4
  • 20
    • 0035446965 scopus 로고    scopus 로고
    • Biochemical characterization of the β-1,4-glucuronosyltransferase GelK in gellan-gum producing strain Sphingomonas paucimobilis A.T.C.C. 31461
    • Videira, P. A., Fialho, A. M., Geremia, R. A., Breton, C. and Sá-Correia, I. (2001) Biochemical characterization of the β-1,4-glucuronosyltransferase GelK in gellan-gum producing strain Sphingomonas paucimobilis A.T.C.C. 31461. Biochem. J. 358, 457-464
    • (2001) Biochem. J. , vol.358 , pp. 457-464
    • Videira, P.A.1    Fialho, A.M.2    Geremia, R.A.3    Breton, C.4    Sá-Correia, I.5
  • 21
    • 0036801506 scopus 로고    scopus 로고
    • Gellan gum biosynthesis in Sphingomonas paucimobilis ATCC 31461: Genes, enzymes and exopolysaccharide production engineering
    • Sá-Correia, I., Fialho, A. M., Videira, P., Moreira, L. M., Marques, A. R. and Albano, H. (2002) Gellan gum biosynthesis in Sphingomonas paucimobilis ATCC 31461: genes, enzymes and exopolysaccharide production engineering. J. Ind. Microbiol. Biotechnol. 29, 170-176
    • (2002) J. Ind. Microbiol. Biotechnol. , vol.29 , pp. 170-176
    • Sá-Correia, I.1    Fialho, A.M.2    Videira, P.3    Moreira, L.M.4    Marques, A.R.5    Albano, H.6
  • 22
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H. C. and Doly, J. (1979) A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7, 1513-1523
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 24
    • 0031039255 scopus 로고    scopus 로고
    • Expression, inducer spectrum, domain structure and function of MopR, the regulator of phenol degradation in Acinetobacter calcoaceticus
    • Schirmer, F., Ehrt, S. and Hillen, W. (1997) Expression, inducer spectrum, domain structure and function of MopR, the regulator of phenol degradation in Acinetobacter calcoaceticus. J. Bacteriol. 179, 1329-1336
    • (1997) J. Bacteriol. , vol.179 , pp. 1329-1336
    • Schirmer, F.1    Ehrt, S.2    Hillen, W.3
  • 25
    • 0030269967 scopus 로고    scopus 로고
    • Development of a simple method for the recovery of recombinant proteins from the Escherichia coli periplasm
    • French, C., Keshavarz-Moore, E. and Ward, J. (1996) Development of a simple method for the recovery of recombinant proteins from the Escherichia coli periplasm. Enzyme Microb. Technol. 19, 332-338
    • (1996) Enzyme Microb. Technol. , vol.19 , pp. 332-338
    • French, C.1    Keshavarz-Moore, E.2    Ward, J.3
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0020475449 scopus 로고
    • A Simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R. F. (1982) A Simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-142
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-142
    • Kyte, J.1    Doolittle, R.F.2
  • 29
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • Frishman, P and Argos, P. (1995) Knowledge-based protein secondary structure assignment. Proteins 23, 566-579
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, P.1    Argos, P.2
  • 31
    • 0031766401 scopus 로고    scopus 로고
    • HOMSTRAD: A database of protein structure alignments for homologous families
    • Mizuguchi, K., Deane, C. M., Blundell, T. L. and Overington, J. P. (1998) HOMSTRAD: a database of protein structure alignments for homologous families. Protein Sci. 7, 2469-2471
    • (1998) Protein Sci. , vol.7 , pp. 2469-2471
    • Mizuguchi, K.1    Deane, C.M.2    Blundell, T.L.3    Overington, J.P.4
  • 32
    • 0027732016 scopus 로고
    • DCSE, an interactive tool for sequence and secondary structure research
    • De Rijk, P. and Wachter, R. De (1993) DCSE, an interactive tool for sequence and secondary structure research. Comput. Appl. Biosci. 9, 735-740
    • (1993) Comput. Appl. Biosci. , vol.9 , pp. 735-740
    • De Rijk, P.1    De Wachter, R.2
  • 33
    • 0025129872 scopus 로고
    • Procedures to derive structural and functional information from 2-D representation of protein sequences
    • Lemesle-Verloot, L., Henrissat, B., Garboriaud, C., Bissery, V., Morgat, A. and Mornon, J.-P. (1990) Procedures to derive structural and functional information from 2-D representation of protein sequences. Biochime 72, 555-574
    • (1990) Biochime , vol.72 , pp. 555-574
    • Lemesle-Verloot, L.1    Henrissat, B.2    Garboriaud, C.3    Bissery, V.4    Morgat, A.5    Mornon, J.-P.6
  • 34
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G. and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 35
    • 0028509254 scopus 로고
    • TREECON for Windows: A software package for the construction and drawing of evolutionary trees for the Microsoft Windows environment
    • Van de Peer, Y. and De Wachter, R. (1994) TREECON for Windows: a software package for the construction and drawing of evolutionary trees for the Microsoft Windows environment. CABIOS Comput. Appl. Biosci. 10, 569-570
    • (1994) CABIOS Comput. Appl. Biosci. , vol.10 , pp. 569-570
    • Van De Peer, Y.1    De Wachter, R.2
  • 36
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N. and Nei, M. (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4, 406-425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 37
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Felsenstein, J. (1985) Confidence limits on phylogenies: an approach using the bootstrap. Evolution 39, 783-791
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 38
    • 0029914954 scopus 로고    scopus 로고
    • Linkage of genes essential for synthesis of a polysaccharide capsule in Sphingomonas strain S88
    • Yamazaki, M., Thorne, L., Mikolajczak, M., Armentrout, R. W. and Pollock, T. J. (1996) Linkage of genes essential for synthesis of a polysaccharide capsule in Sphingomonas strain S88. J. Bacteriol. 178, 2676-2687
    • (1996) J. Bacteriol. , vol.178 , pp. 2676-2687
    • Yamazaki, M.1    Thorne, L.2    Mikolajczak, M.3    Armentrout, R.W.4    Pollock, T.J.5
  • 39
    • 0033018230 scopus 로고    scopus 로고
    • Cloning and expression of the algL gene, encoding the Azotobacter chroococcum alginate lyase: Purification and characterization of the enzyme
    • Peciña, A., Pascual, A. and Paneque, A. (1999) Cloning and expression of the algL gene, encoding the Azotobacter chroococcum alginate lyase: purification and characterization of the enzyme. J. Bacteriol. 181, 1409-1414
    • (1999) J. Bacteriol. , vol.181 , pp. 1409-1414
    • Peciña, A.1    Pascual, A.2    Paneque, A.3
  • 40
    • 0032559380 scopus 로고    scopus 로고
    • Crystal structure of β-glucosidase A from Bacillus polymyxa: Insights into the catalytic activity in family 1 glycosyl hydrolases
    • Sanz-Aparicio, J., Hermoso, J. A., Martinez-Ripoll, M., Lequerica, J. L. and Polaina, J. (1998) Crystal structure of β-glucosidase A from Bacillus polymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases. J. Mol. Biol. 275, 491-502
    • (1998) J. Mol. Biol. , vol.275 , pp. 491-502
    • Sanz-Aparicio, J.1    Hermoso, J.A.2    Martinez-Ripoll, M.3    Lequerica, J.L.4    Polaina, J.5
  • 41
    • 0037177261 scopus 로고    scopus 로고
    • Substrate specificity engineering of β-mannosidase and β-glucosidase from Pyrococcus by exchange of unique active site residues
    • Kaper, T., van Heusden, H. H., van Loo, B., Vasella, A., van der Oost, J. and de Vos, W. M. (2002) Substrate specificity engineering of β-mannosidase and β-glucosidase from Pyrococcus by exchange of unique active site residues. Biochemistry 41, 4147-4155
    • (2002) Biochemistry , vol.41 , pp. 4147-4155
    • Kaper, T.1    Van Heusden, H.H.2    Van Loo, B.3    Vasella, A.4    Van Der Oost, J.5    De Vos, W.M.6
  • 42
    • 0037008171 scopus 로고    scopus 로고
    • Substrate distortion by a β-mannanase: Snapshots of the Michaelis and covalent-intermediate complexes suggest a β(2,5) conformation for the transition state
    • Ducros, V. M., Zechel, D. L., Murshudov, G. N., Gilbert, H. J., Szabo, L., Stoll, D., Withers, S. G. and Davies, G. J. (2002) Substrate distortion by a β-mannanase: snapshots of the Michaelis and covalent-intermediate complexes suggest a β(2,5) conformation for the transition state. Angew. Chem. Int. Ed. 41, 2824-2827
    • (2002) Angew. Chem. Int. Ed. , vol.41 , pp. 2824-2827
    • Ducros, V.M.1    Zechel, D.L.2    Murshudov, G.N.3    Gilbert, H.J.4    Szabo, L.5    Stoll, D.6    Withers, S.G.7    Davies, G.J.8
  • 43
    • 0031904682 scopus 로고    scopus 로고
    • Sequence, structural, functional, and phylogenetic analyses of three glycosidase families
    • Mian, I. S. (1998) Sequence, structural, functional, and phylogenetic analyses of three glycosidase families. Blood Cell Mol. Dis. 24, 83-100
    • (1998) Blood Cell Mol. Dis. , vol.24 , pp. 83-100
    • Mian, I.S.1
  • 44
    • 0026755998 scopus 로고
    • Cloning and expression in Escherichia coli of a Streptomyces β-glucosidase gene
    • Mastromei, G., Hanhart, E., Perito, B. and Polsinelli, M. (1992) Cloning and expression in Escherichia coli of a Streptomyces β-glucosidase gene. J. Biotech. 24, 149-157
    • (1992) J. Biotech. , vol.24 , pp. 149-157
    • Mastromei, G.1    Hanhart, E.2    Perito, B.3    Polsinelli, M.4
  • 45
    • 0029033496 scopus 로고
    • Cloning and nucleotide sequence of the bglA gene from Erwinia herbicola and expression of β-glucosidase activity in Escherichia coli
    • Marri, L., Valentini, S. and Venditti, D. (1995) Cloning and nucleotide sequence of the bglA gene from Erwinia herbicola and expression of β-glucosidase activity in Escherichia coli. FEMS Microbiol. Lett. 128, 135-138
    • (1995) FEMS Microbiol. Lett. , vol.128 , pp. 135-138
    • Marri, L.1    Valentini, S.2    Venditti, D.3
  • 46
    • 0033028398 scopus 로고    scopus 로고
    • Pseudomonas syringae phytotoxins: Mode of action, regulation, and biosynthesis by peptide and polyketide synthetases
    • Bender, C. L., Alarcon-Chaidez, F. and Gross, D. C. (1999) Pseudomonas syringae phytotoxins: mode of action, regulation, and biosynthesis by peptide and polyketide synthetases. Microbiol. Mol. Biol. Rev. 63, 266-292
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 266-292
    • Bender, C.L.1    Alarcon-Chaidez, F.2    Gross, D.C.3
  • 48
    • 0031662992 scopus 로고    scopus 로고
    • Hairy plant polysaccharides: A close shave with microbial esterases
    • Williamson, G., Kroon, P. A. and Faulds, C. B. (1998) Hairy plant polysaccharides: a close shave with microbial esterases. Microbiology 144, 2011-2023
    • (1998) Microbiology , vol.144 , pp. 2011-2023
    • Williamson, G.1    Kroon, P.A.2    Faulds, C.B.3
  • 49
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat, B. and Bairoch, A. (1996) Updating the sequence-based classification of glycosyl hydrolases. Biochem. J. 316, 695-696
    • (1996) Biochem. J. , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 50
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycosyl hydrolases
    • Henrissat, B. and Davies, G. (1997) Structural and sequence-based classification of glycosyl hydrolases. Curr. Opin. Struct. Biol. 7, 637-644
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 51
    • 0026731191 scopus 로고
    • Region-directed mutagenesis of residues surrounding the active site nucleophile in β-glucosidase from Agrobacterium faecalis
    • Trimbur, D. E., Warren, R. A. and Withers, S. G. (1992) Region-directed mutagenesis of residues surrounding the active site nucleophile in β-glucosidase from Agrobacterium faecalis. J. Biol. Chem. 267, 10248-10251
    • (1992) J. Biol. Chem. , vol.267 , pp. 10248-10251
    • Trimbur, D.E.1    Warren, R.A.2    Withers, S.G.3
  • 52
    • 0029392961 scopus 로고
    • Families, superfamllies and subfamilies of glycosyl hydrolases
    • Henrissat, B. and Romeu, A. (1995) Families, superfamllies and subfamilies of glycosyl hydrolases. Biochem. J. 311, 350-351
    • (1995) Biochem. J. , vol.311 , pp. 350-351
    • Henrissat, B.1    Romeu, A.2
  • 53
    • 0033670249 scopus 로고    scopus 로고
    • Horizontal gene transfer of glycosyl hydrolases of the rumen fungi
    • Garcia-Vallvé, S., Romeu, A. and Palau, J. (2000) Horizontal gene transfer of glycosyl hydrolases of the rumen fungi. Genome Res. 10, 1719-1725
    • (2000) Genome Res. , vol.10 , pp. 1719-1725
    • Garcia-Vallvé, S.1    Romeu, A.2    Palau, J.3
  • 54
    • 0034870609 scopus 로고    scopus 로고
    • A census of carbohydrate-active enzymes in the genome of Arabidopsis thaliana
    • Henrissat, B., Coutinho, P. M. and Davies, G. J. (2001) A census of carbohydrate-active enzymes in the genome of Arabidopsis thaliana. Plant Mol. Biol. 47, 55-72
    • (2001) Plant Mol. Biol. , vol.47 , pp. 55-72
    • Henrissat, B.1    Coutinho, P.M.2    Davies, G.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.