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Volumn 68, Issue 5, 2004, Pages 1113-1118

Effects of truncation at the non-homologous region of a family 3 β-glucosidase from Agrobacterium tumefaciens

Author keywords

Agrobacterium tumefaciens; Family 3 glucosidase; Transglycosylation; Truncated mutant

Indexed keywords

BETA GLUCOSIDASE;

EID: 4544331931     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.68.1113     Document Type: Article
Times cited : (7)

References (14)
  • 1
    • 0025321899 scopus 로고
    • Identification of an Agrobacterium tumefaciens virulence gene inducer from the pinaceous gymnosperm Pseudotsuga menziesii
    • Morris, J. W., and Morris, R. O., Identification of an Agrobacterium tumefaciens virulence gene inducer from the pinaceous gymnosperm Pseudotsuga menziesii. Proc. Natl. Acad. Sci. U.S.A., 87, 3614-3618 (1990).
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 3614-3618
    • Morris, J.W.1    Morris, R.O.2
  • 2
    • 0026521573 scopus 로고
    • Cloning and sequencing of an Agrobacterium tumefaciens β-glucosidase gene involved in modifying a vir-inducing plant signal molecule
    • Castle, L. A., Smith, K. D., and Morris, R. O., Cloning and sequencing of an Agrobacterium tumefaciens β-glucosidase gene involved in modifying a vir-inducing plant signal molecule. J. Bacteriol., 174, 1478-1486 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 1478-1486
    • Castle, L.A.1    Smith, K.D.2    Morris, R.O.3
  • 3
    • 0031834858 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens β-glucosidase is also an effective β-xylosidase, and has a high transglycosylation activity in the presence of alcohols
    • Watt, D. K., Ono, H., and Hayashi, K., Agrobacterium tumefaciens β-glucosidase is also an effective β-xylosidase, and has a high transglycosylation activity in the presence of alcohols. Biochim. Biophys. Acta, 1385, 78-88 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 78-88
    • Watt, D.K.1    Ono, H.2    Hayashi, K.3
  • 4
    • 0033081517 scopus 로고    scopus 로고
    • Three-dimensional structure of a barley β-D-glucan exohydrolase, a family 3 glycosyl hydrolase
    • Varghese, J. N., Hrmova, M., and Fincher, G. B., Three-dimensional structure of a barley β-D-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure, 7, 179-190 (1999).
    • (1999) Structure , vol.7 , pp. 179-190
    • Varghese, J.N.1    Hrmova, M.2    Fincher, G.B.3
  • 5
    • 0035183914 scopus 로고    scopus 로고
    • Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant β-D-glucan glucohydrolase
    • Hrmova, M., Varghese, J. N., DeGori, R., Smith, B. J., Driguez, H., and Fincher, G. B., Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant β-D-glucan glucohydrolase. Structure, 9, 1005-1016 (2001).
    • (2001) Structure , vol.9 , pp. 1005-1016
    • Hrmova, M.1    Varghese, J.N.2    Degori, R.3    Smith, B.J.4    Driguez, H.5    Fincher, G.B.6
  • 6
    • 0028982269 scopus 로고
    • Construction of chimeric β-glucosidase with improved enzymatic properties
    • Singh, A., and Hayashi, K., Construction of chimeric β-glucosidase with improved enzymatic properties. J. Biol. Chem., 270, 21928-21933 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 21928-21933
    • Singh, A.1    Hayashi, K.2
  • 7
    • 0035923379 scopus 로고    scopus 로고
    • Construction and characterization of chimeric enzymes of the Agrobacterium tumefaciens and Thermotoga maritima β-glucosidases
    • Goyal, K., Kim, Y.-K., Kitaoka, M., and Hayashi, K., Construction and characterization of chimeric enzymes of the Agrobacterium tumefaciens and Thermotoga maritima β-glucosidases. J. Mol. Catal. B: Enzym., 16, 43-51 (2001).
    • (2001) J. Mol. Catal. B: Enzym. , vol.16 , pp. 43-51
    • Goyal, K.1    Kim, Y.-K.2    Kitaoka, M.3    Hayashi, K.4
  • 8
    • 0028955590 scopus 로고
    • Construction and characterization of a chimeric β-glucosidase
    • Singh, A., Hayashi, K., Hoa, T. T., Kashiwagi, Y., and Tokuyasu, K., Construction and characterization of a chimeric β-glucosidase. Biochem. J., 305, 715-719 (1995).
    • (1995) Biochem. J. , vol.305 , pp. 715-719
    • Singh, A.1    Hayashi, K.2    Hoa, T.T.3    Kashiwagi, Y.4    Tokuyasu, K.5
  • 9
    • 0036407598 scopus 로고    scopus 로고
    • Enhancement of transglycosylation activity by construction of chimeras between mesophilic and thermophilic β-glucosidase
    • Goyal, K., Kim, B. J., Kim, J.-D., Kim, Y.-K., Kitaoka, M., and Hayashi, K., Enhancement of transglycosylation activity by construction of chimeras between mesophilic and thermophilic β-glucosidase. Arch. Biochem. Biophys., 407, 125-134 (2002).
    • (2002) Arch. Biochem. Biophys. , vol.407 , pp. 125-134
    • Goyal, K.1    Kim, B.J.2    Kim, J.-D.3    Kim, Y.-K.4    Kitaoka, M.5    Hayashi, K.6
  • 10
    • 0027406360 scopus 로고
    • The nucleotide sequence of the β-glucosidase gene from Cellvibrio gilvus
    • Kashiwagi, Y., Aoyagi, C., Sasaki, T., and Taniguchi, H., The nucleotide sequence of the β-glucosidase gene from Cellvibrio gilvus. J. Ferment. Bioeng., 75, 159-165 (1993).
    • (1993) J. Ferment. Bioeng. , vol.75 , pp. 159-165
    • Kashiwagi, Y.1    Aoyagi, C.2    Sasaki, T.3    Taniguchi, H.4
  • 11
    • 0035965060 scopus 로고    scopus 로고
    • Characterization of a thermostable β-glucosidase (BglB) from Thermotoga maritima showing transglycosylation activity
    • Goyal, K., Selvakumar, P., and Hayashi, K., Characterization of a thermostable β-glucosidase (BglB) from Thermotoga maritima showing transglycosylation activity. J. Mol. Catal. B: Enzym., 15, 45-53 (2001).
    • (2001) J. Mol. Catal. B: Enzym. , vol.15 , pp. 45-53
    • Goyal, K.1    Selvakumar, P.2    Hayashi, K.3
  • 12
    • 0032008243 scopus 로고    scopus 로고
    • Overproduction of β-glucosidase in active form by an Escherichia coli system coexpressing the chaperonin GroEL/ES
    • Machida, S., Yu, Y., Singh, S. P., Kim, J.-D., Hayashi, K., and Kawata, Y., Overproduction of β-glucosidase in active form by an Escherichia coli system coexpressing the chaperonin GroEL/ES. FEMS Microbiol. Lett., 159, 41-46 (1998).
    • (1998) FEMS Microbiol. Lett. , vol.159 , pp. 41-46
    • Machida, S.1    Yu, Y.2    Singh, S.P.3    Kim, J.-D.4    Hayashi, K.5    Kawata, Y.6
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.