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Volumn 8, Issue 5, 2001, Pages 437-443

Directed evolution of new glycosynthases from Agrobacterium β-glucosidase: A general screen to detect enzymes for oligosaccharide synthesis

Author keywords

Directed evolution; Enzymatic oligosaccharide synthesis; Glycosyl transfer; Glycosynthase

Indexed keywords

AGAR; BACTERIAL ENZYME; BETA GLUCOSIDASE; CATALYST ACTIVITY; ENZYME ENGINEERING; ENZYME; EVOLUTION; GLYCOSYLTRANSFERASE; GLYCOSYNTHASE; INDUSTRIAL ENZYME; OLIGOSACCHARIDE; SCREENING;

EID: 0034999624     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(01)00022-9     Document Type: Article
Times cited : (101)

References (30)
  • 1
    • 0034599121 scopus 로고    scopus 로고
    • From the laboratory to the clinic: A retrospective on fully synthetic carbohydrate-based anticancer vaccines
    • S.J. Danishefsky, J.R. Allen, From the laboratory to the clinic: A retrospective on fully synthetic carbohydrate-based anticancer vaccines, Angew. Chem. Int. Ed. Engl. 39 (2000) 837-863.
    • (2000) Angew. Chem. Int. Ed. Engl. , vol.39 , pp. 837-863
    • Danishefsky, S.J.1    Allen, J.R.2
  • 2
    • 0034092365 scopus 로고    scopus 로고
    • Emerging roles of carbohydrates and glycomimetics in anticancer drug design
    • J.J. Barchi, Emerging roles of carbohydrates and glycomimetics in anticancer drug design, Curr. Pharm. Design 6 (2000) 485-501.
    • (2000) Curr. Pharm. Design , vol.6 , pp. 485-501
    • Barchi, J.J.1
  • 3
    • 0000084638 scopus 로고    scopus 로고
    • Carbohydrate drugs - An ongoing challenge
    • J.C. McAuliffe, O. Hindsgaul, Carbohydrate drugs - An ongoing challenge, Chem. Ind. 5 (1997) 170-174.
    • (1997) Chem. Ind. , vol.5 , pp. 170-174
    • McAuliffe, J.C.1    Hindsgaul, O.2
  • 4
    • 0033964068 scopus 로고    scopus 로고
    • Enzyme-catalyzed synthesis of carbohydrates
    • N. Wymer, E.J. Toone, Enzyme-catalyzed synthesis of carbohydrates, Curr. Opin. Chem. Biol. 4 (2000) 110-119.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 110-119
    • Wymer, N.1    Toone, E.J.2
  • 5
    • 0032708956 scopus 로고    scopus 로고
    • Biocatalytic synthesis of oligosaccharides
    • M.M. Palcic, Biocatalytic synthesis of oligosaccharides, Curr. Opin. Biotechnol. 10 (1999) 616-624.
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 616-624
    • Palcic, M.M.1
  • 6
    • 0031870803 scopus 로고    scopus 로고
    • Cost-effective carbohydrate synthesis permits large-scale production of an anti-inflammatory drug
    • C. Sansom, Cost-effective carbohydrate synthesis permits large-scale production of an anti-inflammatory drug, Mol. Med. Today 4 (1998) 322.
    • (1998) Mol. Med. Today , vol.4 , pp. 322
    • Sansom, C.1
  • 7
    • 0026655074 scopus 로고
    • Enzyme-catalyzed oligosaccharide synthesis
    • Y. Ichikawa, G.C. Look, C.H. Wong, Enzyme-catalyzed oligosaccharide synthesis, Anal. Biochem. 202 (1992) 215-238.
    • (1992) Anal. Biochem. , vol.202 , pp. 215-238
    • Ichikawa, Y.1    Look, G.C.2    Wong, C.H.3
  • 8
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • B. Henrissat, A. Bairoch, Updating the sequence-based classification of glycosyl hydrolases, Biochem. J. 316 (1996) 695-696.
    • (1996) Biochem. J. , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 9
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • B. Henrissat, A. Bairoch, New families in the classification of glycosyl hydrolases based on amino acid sequence similarities, Biochem. J. 293 (1993) 781-788.
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 10
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • B. Henrissat, A classification of glycosyl hydrolases based on amino acid sequence similarities, Biochem. J. 280 (1991) 309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 11
    • 0342387579 scopus 로고    scopus 로고
    • http://afmb.cnrs-mrs.fr/~pedro/.
  • 14
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymatic glycosyl transfer
    • M.L. Sinnott, Catalytic mechanisms of enzymatic glycosyl transfer, Chem. Rev. 90 (1990) 1171-1202.
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 15
    • 0001410590 scopus 로고
    • Identification of a covalent α-D-glucopyranosyl enzyme intermediate formed on a β-glucosidase
    • S.G. Withers, I.P. Street, Identification of a covalent α-D-glucopyranosyl enzyme intermediate formed on a β-glucosidase, J. Am. Chem. Soc. 110 (1988) 8551-8553.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 8551-8553
    • Withers, S.G.1    Street, I.P.2
  • 16
    • 0030052194 scopus 로고    scopus 로고
    • Crystallographic observation of a covalent catalytic intermediate in a β-glycosidase
    • A. White, D. Tull, K. Johns, S.G. Withers, D.R. Rose, Crystallographic observation of a covalent catalytic intermediate in a β-glycosidase, Nature Struct. Biol. 3 (1996) 149-154.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 149-154
    • White, A.1    Tull, D.2    Johns, K.3    Withers, S.G.4    Rose, D.R.5
  • 17
    • 0026785573 scopus 로고
    • Inactivation of a β-glucosidase through the accumulation of a stable 2-deoxy-2-fluoro-α-D-glucopyranosyl-enzyme intermediate: A detailed investigation
    • I.P. Street, J.B. Kempton, S.G. Withers, Inactivation of a β-glucosidase through the accumulation of a stable 2-deoxy-2-fluoro-α-D-glucopyranosyl-enzyme intermediate: a detailed investigation, Biochemistry 31 (1992) 9970-9978.
    • (1992) Biochemistry , vol.31 , pp. 9970-9978
    • Street, I.P.1    Kempton, J.B.2    Withers, S.G.3
  • 18
    • 0031715607 scopus 로고    scopus 로고
    • Insights into transition state stabilization of the β-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutants
    • V. Notenboom, C. Birsan, M. Nitz, D.R. Rose, R.A. Warren, S.G. Withers, Insights into transition state stabilization of the β-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutants, Nature Struct. Biol. 5 (1998) 812-818.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 812-818
    • Notenboom, V.1    Birsan, C.2    Nitz, M.3    Rose, D.R.4    Warren, R.A.5    Withers, S.G.6
  • 19
  • 20
    • 0033954715 scopus 로고    scopus 로고
    • The E358S mutant of Agrobacterium sp. β-glucosidase is a greatly improved glycosynthase
    • C. Mayer, D.L. Zechel, S.P. Reid, R.A.J. Warren, S.G. Withers, The E358S mutant of Agrobacterium sp. β-glucosidase is a greatly improved glycosynthase, FEBS Lett. 466 (2000) 40-44.
    • (2000) FEBS Lett. , vol.466 , pp. 40-44
    • Mayer, C.1    Zechel, D.L.2    Reid, S.P.3    Warren, R.A.J.4    Withers, S.G.5
  • 21
    • 0032573586 scopus 로고    scopus 로고
    • From β-glucanase to β-glucansynthase: Glycosyl transfer to α-glycosyl fluorides catalyzed by a mutant endoglucanase lacking its catalytic nucleophile
    • C. Malet, A. Planas, From β-glucanase to β-glucansynthase: glycosyl transfer to α-glycosyl fluorides catalyzed by a mutant endoglucanase lacking its catalytic nucleophile, FEBS Lett. 440 (1998) 208-212.
    • (1998) FEBS Lett. , vol.440 , pp. 208-212
    • Malet, C.1    Planas, A.2
  • 22
    • 0034696084 scopus 로고    scopus 로고
    • A novel thermophilic glycosynthase that effects branching glycosylation
    • A. Trincone, G. Perugino, M. Rossi, M. Moracci, A novel thermophilic glycosynthase that effects branching glycosylation, Bioorg. Med. Chem. Lett. 10 (2000) 365-368.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 365-368
    • Trincone, A.1    Perugino, G.2    Rossi, M.3    Moracci, M.4
  • 24
    • 0032518266 scopus 로고    scopus 로고
    • DNA shuffling of a family of genes from diverse species accelerates directed evolution
    • A. Crameri, S.A. Raillard, E. Bermudez, W.P.C. Stemmer, DNA shuffling of a family of genes from diverse species accelerates directed evolution, Nature 391 (1998) 288-291.
    • (1998) Nature , vol.391 , pp. 288-291
    • Crameri, A.1    Raillard, S.A.2    Bermudez, E.3    Stemmer, W.P.C.4
  • 27
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in-vitro by DNA shuffling
    • W.P.C. Stemmer, Rapid evolution of a protein in-vitro by DNA shuffling, Nature 370 (1994) 389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 28
    • 0030989062 scopus 로고    scopus 로고
    • Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening
    • J.H. Zhang, G. Dawes, W.P.C. Stemmer, Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening, Proc. Natl. Acad. Sci. USA 94 (1997) 4504-4509.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4504-4509
    • Zhang, J.H.1    Dawes, G.2    Stemmer, W.P.C.3
  • 29
    • 0029896866 scopus 로고    scopus 로고
    • Characterization of CenC, an enzyme from Cellulomonas fimi with both endo- and exoglucanase activities
    • P. Tomme, E. Kwan, N.R. Gilkes, D.G. Kilburn, R.A. Warren, Characterization of CenC, an enzyme from Cellulomonas fimi with both endo- and exoglucanase activities, J. Bacteriol. 178 (1996) 4216-4223.
    • (1996) J. Bacteriol. , vol.178 , pp. 4216-4223
    • Tomme, P.1    Kwan, E.2    Gilkes, N.R.3    Kilburn, D.G.4    Warren, R.A.5
  • 30
    • 0027401279 scopus 로고
    • Cellulose-binding polypeptides from Cellulomonas fimi - Endoglucanase-D (Cend), a family a β-1,4-glucanase
    • A. Meinke, N.R. Gilkes, D.G. Kilburn, R.C. Miller, R.A.J. Warren, Cellulose-binding polypeptides from Cellulomonas fimi - endoglucanase-D (Cend), a family A β-1,4-glucanase, J. Bacteriol. 175 (1993) 1910-1918.
    • (1993) J. Bacteriol. , vol.175 , pp. 1910-1918
    • Meinke, A.1    Gilkes, N.R.2    Kilburn, D.G.3    Miller, R.C.4    Warren, R.A.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.