메뉴 건너뛰기




Volumn 10, Issue 7, 2003, Pages 619-628

Anatomy of glycosynthesis: Structure and kinetics of the Humicola insolens Cel7B E197A and E197S glycosynthase mutants

Author keywords

[No Author keywords available]

Indexed keywords

FUNGI; HUMICOLA; HUMICOLA INSOLENS;

EID: 0041629327     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(03)00143-1     Document Type: Article
Times cited : (67)

References (54)
  • 1
    • 0001094662 scopus 로고    scopus 로고
    • Glycobiology: Toward understanding the function of sugars
    • Dwek R.A. Glycobiology. toward understanding the function of sugars Chem. Rev. 96:1996;683-720.
    • (1996) Chem. Rev. , vol.96 , pp. 683-720
    • Dwek, R.A.1
  • 2
    • 0035937499 scopus 로고    scopus 로고
    • Chemical glycobiology
    • Bertozzi C.R., Kiessling L.L. Chemical glycobiology. Science. 291:2001;2357-2364.
    • (2001) Science , vol.291 , pp. 2357-2364
    • Bertozzi, C.R.1    Kiessling, L.L.2
  • 4
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: Signal transduction and O-GlcNAc
    • Wells L., Vosseller K., Hart G.W. Glycosylation of nucleocytoplasmic proteins. signal transduction and O-GlcNAc Science. 291:2001;2376-2378.
    • (2001) Science , vol.291 , pp. 2376-2378
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 5
    • 0037127198 scopus 로고    scopus 로고
    • Dynamic O-glycosylation of nuclear and cytosolic proteins: Further characterization of the nucleocytoplasmic beta-N-acetylglucosaminidase, O-GlcNAcase
    • Wells L., Gao Y., Mahoney J.A., Vosseller K., Chen C., Rosen A., Hart G.W. Dynamic O-glycosylation of nuclear and cytosolic proteins. further characterization of the nucleocytoplasmic beta-N-acetylglucosaminidase, O-GlcNAcase J. Biol. Chem. 277:2002;1755-1761.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1755-1761
    • Wells, L.1    Gao, Y.2    Mahoney, J.A.3    Vosseller, K.4    Chen, C.5    Rosen, A.6    Hart, G.W.7
  • 6
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies G.J., Wilson K.S., Henrissat B. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem. J. 321:1997;557-559.
    • (1997) Biochem. J. , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 7
    • 0032708956 scopus 로고    scopus 로고
    • Biocatalytic synthesis of oligosaccharides
    • Palcic M.M. Biocatalytic synthesis of oligosaccharides. Curr. Opin. Biotechnol. 10:1999;616-624.
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 616-624
    • Palcic, M.M.1
  • 8
    • 0031993483 scopus 로고    scopus 로고
    • Glycosidases and glycosyl transferases in glycoside and oligosaccharide synthesis
    • Crout H.G., Vic G. Glycosidases and glycosyl transferases in glycoside and oligosaccharide synthesis. Curr. Opin. Chem. Biol. 2:1998;98-111.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 98-111
    • Crout, H.G.1    Vic, G.2
  • 9
    • 84961309849 scopus 로고    scopus 로고
    • Glycosidase catalysed oligosaccharide synthesis
    • B. Ernst, G.W. Hart, & P. Sinay. Weinheim, Germany: Wiley-VCH GmbH. 723-844.pp
    • Vocadlo D.J., Withers S.G. Glycosidase catalysed oligosaccharide synthesis. Ernst B., Hart G.W., Sinay P. Carbohydrates in Chemistry and Biology, Volume 2. 2000;Wiley-VCH GmbH, Weinheim, Germany. 723-844.pp.
    • (2000) Carbohydrates in Chemistry and Biology, Volume 2
    • Vocadlo, D.J.1    Withers, S.G.2
  • 10
    • 0032503519 scopus 로고    scopus 로고
    • Glycosynthases: Mutant glycosidases for oligosaccharide synthesis
    • Mackenzie L.F., Wang Q., Warren R.A.J., Withers S.G. Glycosynthases. mutant glycosidases for oligosaccharide synthesis J. Am. Chem. Soc. 120:1998;5583-5584.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 5583-5584
    • Mackenzie, L.F.1    Wang, Q.2    Warren, R.A.J.3    Withers, S.G.4
  • 11
    • 0032573586 scopus 로고    scopus 로고
    • From β-glucanase to β-glucansynthase: Glycosyl transfer to α-glycosyl fluorides by a mutant endoglucanase lacking its catalytic nucleophile
    • Malet C., Planas A. From β-glucanase to β-glucansynthase. glycosyl transfer to α-glycosyl fluorides 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
  • 13
    • 0034696084 scopus 로고    scopus 로고
    • A novel thermophilic glycosynthase that effects branching glycosylation
    • Trincone A., Perugino G., Rossi M., Moracci M. 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
  • 14
    • 0035813818 scopus 로고    scopus 로고
    • Oligosaccharide synthesis by coupled endo-glycosynthases of different specificity: A straightforward preparation of two mixed-linkage hexasaccharide substrates of 1,3/1,4-beta-glucanases
    • Faijes M., Fairweather J.K., Driguez H., Planas A. Oligosaccharide synthesis by coupled endo-glycosynthases of different specificity. a straightforward preparation of two mixed-linkage hexasaccharide substrates of 1,3/1,4-beta-glucanases Chemistry. 7:2001;4651-4655.
    • (2001) Chemistry , vol.7 , pp. 4651-4655
    • Faijes, M.1    Fairweather, J.K.2    Driguez, H.3    Planas, A.4
  • 16
    • 0037087494 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of a bifunctionalized cellohexaoside as a specific substrate for the sensitive assay of cellulase by fluorescence quenching
    • Boyer V., Fort S., Frandsen T.P., Schulein M., Cottaz S., Driguez H. Chemoenzymatic synthesis of a bifunctionalized cellohexaoside as a specific substrate for the sensitive assay of cellulase by fluorescence quenching. Chemistry. 8:2002;1389-1394.
    • (2002) Chemistry , vol.8 , pp. 1389-1394
    • Boyer, V.1    Fort, S.2    Frandsen, T.P.3    Schulein, M.4    Cottaz, S.5    Driguez, H.6
  • 19
    • 0032532639 scopus 로고    scopus 로고
    • Crystal structure of the family 7 endoglucanase I (Cel7B) from Humicola insolens at 2.2 Å resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate
    • Mackenzie L.F., Sulzenbacher G., Divne C., Jones T.A., Woldike H.F., Schülein M., Withers S.G., Davies G.J. Crystal structure of the family 7 endoglucanase I (Cel7B) from Humicola insolens at 2.2 Å resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate. Biochem. J. 335:1998;409-416.
    • (1998) Biochem. J. , vol.335 , pp. 409-416
    • Mackenzie, L.F.1    Sulzenbacher, G.2    Divne, C.3    Jones, T.A.4    Woldike, H.F.5    Schülein, M.6    Withers, S.G.7    Davies, G.J.8
  • 20
    • 0033954715 scopus 로고    scopus 로고
    • The E358S mutant of Agrobacterium sp. β-glucosidase is a greatly improved glycosynthase
    • Mayer C., Zechel D.L., Reid S.P., Warren R.A.J., Withers S.G. 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
  • 22
    • 0036436302 scopus 로고    scopus 로고
    • On expanding the repertoire of glycosynthases: Mutant β-galactosidases forming β-(1,6)-linkages
    • Jakeman D.L., Withers S.G. On expanding the repertoire of glycosynthases. mutant β-galactosidases forming β-(1,6)-linkages Can. J. Chem. 80:2002;866-870.
    • (2002) Can. J. Chem. , vol.80 , pp. 866-870
    • Jakeman, D.L.1    Withers, S.G.2
  • 24
    • 0033559148 scopus 로고    scopus 로고
    • Recent insights into inhibition, structure, and mechanism of configuration-retaining glycosidases
    • Heightman T.D., Vasella A.T. Recent insights into inhibition, structure, and mechanism of configuration-retaining glycosidases. Angew. Chem. Int. Ed. Engl. 38:1999;750-770.
    • (1999) Angew. Chem. Int. Ed. Engl. , vol.38 , pp. 750-770
    • Heightman, T.D.1    Vasella, A.T.2
  • 25
    • 0029856409 scopus 로고    scopus 로고
    • Structure of the fusarium oxysporum endoglucanase i with a nonhydrolyzable substrate analogue: Substrate distortion gives rise to the preferred axial orientation for the leaving group
    • Sulzenbacher G., Driguez H., Henrissat B., Schulein M., Davies G.J. Structure of the fusarium oxysporum endoglucanase i with a nonhydrolyzable substrate analogue. substrate distortion gives rise to the preferred axial orientation for the leaving group Biochemistry. 35:1996;15280-15287.
    • (1996) Biochemistry , vol.35 , pp. 15280-15287
    • Sulzenbacher, G.1    Driguez, H.2    Henrissat, B.3    Schulein, M.4    Davies, G.J.5
  • 26
    • 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
    • Street I.P., Kempton J.B., Withers S.G. 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
  • 27
    • 0026668499 scopus 로고
    • Glu-537, Not Glu-461, is the nucleophile in the active site of (lac Z) β-galactosidase from E. coli
    • Gebler J.C., Aebersold R., Withers S.G. Glu-537, Not Glu-461, is the nucleophile in the active site of (lac Z) β-galactosidase from E. coli. J. Biol. Chem. 267:1992;11126-11130.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11126-11130
    • Gebler, J.C.1    Aebersold, R.2    Withers, S.G.3
  • 28
    • 0026666602 scopus 로고
    • Binding energy and catalysis: Fluorinated and deoxygenated glycosides as mechanistic probes of Escherichia coli (lac Z) β-galactosidase
    • McCarter J., Adam M., Withers S.G. Binding energy and catalysis. fluorinated and deoxygenated glycosides as mechanistic probes of Escherichia coli (lac Z) β-galactosidase Biochem. J. 286:1992;721-727.
    • (1992) Biochem. J. , vol.286 , pp. 721-727
    • McCarter, J.1    Adam, M.2    Withers, S.G.3
  • 29
    • 0032545380 scopus 로고    scopus 로고
    • Identification of Glu-540 as the catalytic nucleophile of human beta-glucuronidase using electrospray mass spectrometry
    • Wong A.W., He S., Grubb J.H., Sly W.S., Withers S.G. Identification of Glu-540 as the catalytic nucleophile of human beta-glucuronidase using electrospray mass spectrometry. J. Biol. Chem. 273:1998;34057-34062.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34057-34062
    • Wong, A.W.1    He, S.2    Grubb, J.H.3    Sly, W.S.4    Withers, S.G.5
  • 30
    • 0034331340 scopus 로고    scopus 로고
    • Identification of Glu-519 as the catalytic nucleophile in β-mannosidase 2A from Cellulomonas fimi
    • Stoll D., He S., Withers S.G., Warren R.A.J. Identification of Glu-519 as the catalytic nucleophile in β-mannosidase 2A from Cellulomonas fimi. Biochem. J. 351:2000;833-838.
    • (2000) Biochem. J. , vol.351 , pp. 833-838
    • Stoll, D.1    He, S.2    Withers, S.G.3    Warren, R.A.J.4
  • 31
    • 0031013203 scopus 로고    scopus 로고
    • Identification of Glu-330 as the catalytic nucleophile of Candida albicans exo-beta-(1,3)-glucanase
    • Mackenzie L.F., Brooke G.S., Cutfield J.F., Sullivan P.A., Withers S.G. Identification of Glu-330 as the catalytic nucleophile of Candida albicans exo-beta-(1,3)-glucanase. J. Biol. Chem. 272:1997;3161-3167.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3161-3167
    • Mackenzie, L.F.1    Brooke, G.S.2    Cutfield, J.F.3    Sullivan, P.A.4    Withers, S.G.5
  • 32
    • 0030947305 scopus 로고    scopus 로고
    • Identification of the catalytic nucleophile of endoglucanase I from Fusarium oxysporum by mass spectrometry
    • Mackenzie L.F., Davies G.J., Schulein M., Withers S.G. Identification of the catalytic nucleophile of endoglucanase I from Fusarium oxysporum by mass spectrometry. Biochemistry. 36:1997;5893-5901.
    • (1997) Biochemistry , vol.36 , pp. 5893-5901
    • Mackenzie, L.F.1    Davies, G.J.2    Schulein, M.3    Withers, S.G.4
  • 33
    • 0028224697 scopus 로고
    • Mechanisms of cellulases and xylanases: A detailed kinetic study of the exo-beta-1,4-glycanase from Cellulomonas fimi
    • Tull D., Withers S.G. Mechanisms of cellulases and xylanases. a detailed kinetic study of the exo-beta-1,4-glycanase from Cellulomonas fimi Biochemistry. 33:1994;6363-6370.
    • (1994) Biochemistry , vol.33 , pp. 6363-6370
    • Tull, D.1    Withers, S.G.2
  • 34
    • 0028244925 scopus 로고
    • Identification of glutamic acid 78 as the active site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass spectrometry
    • Miao S., Ziser L., Aebersold R., Withers S.G. Identification of glutamic acid 78 as the active site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass spectrometry. Biochemistry. 33:1994;7027-7032.
    • (1994) Biochemistry , vol.33 , pp. 7027-7032
    • Miao, S.1    Ziser, L.2    Aebersold, R.3    Withers, S.G.4
  • 35
    • 0032533166 scopus 로고    scopus 로고
    • Identification of Glu-120 as the catalytic nucleophile in Streptomyces lividans endoglucanase CelB
    • Zechel D.L., He S., Dupont C., Withers S.G. Identification of Glu-120 as the catalytic nucleophile in Streptomyces lividans endoglucanase CelB. Biochem. J. 336:1998;139-145.
    • (1998) Biochem. J. , vol.336 , pp. 139-145
    • Zechel, D.L.1    He, S.2    Dupont, C.3    Withers, S.G.4
  • 36
    • 0035933580 scopus 로고    scopus 로고
    • The identification of the catalytic nucleophiles of two beta-galactosidases from glycoside hydrolase family 35
    • Blanchard J.E., Gal L., He S., Foisy J., Warren R.A., Withers S.G. The identification of the catalytic nucleophiles of two beta-galactosidases from glycoside hydrolase family 35. Carbohydr. Res. 333:2001;7-17.
    • (2001) Carbohydr. Res. , vol.333 , pp. 7-17
    • Blanchard, J.E.1    Gal, L.2    He, S.3    Foisy, J.4    Warren, R.A.5    Withers, S.G.6
  • 37
    • 0032532593 scopus 로고    scopus 로고
    • Identification of Glu-277 as the catalytic nucleophile of Thermoanaerobacterium saccharolyticum β-xylosidase using electrospray MS
    • Vocadlo D.J., Mackenzie L.F., He S., Zeikus G.J., Withers S.G. Identification of Glu-277 as the catalytic nucleophile of Thermoanaerobacterium saccharolyticum β-xylosidase using electrospray MS. Biochem. J. 335:1998;449-455.
    • (1998) Biochem. J. , vol.335 , pp. 449-455
    • Vocadlo, D.J.1    Mackenzie, L.F.2    He, S.3    Zeikus, G.J.4    Withers, S.G.5
  • 39
    • 0029876033 scopus 로고    scopus 로고
    • Stereochemical course and reaction products of the action of beta-xylosidase from Thermoanaerobacterium saccharolyticum strain B6A-RI
    • Armand S., Vieille C., Gey C., Heyraud A., Zeikus J.G., Henrissat B. Stereochemical course and reaction products of the action of beta-xylosidase from Thermoanaerobacterium saccharolyticum strain B6A-RI. Eur. J. Biochem. 236:1996;706-713.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 706-713
    • Armand, S.1    Vieille, C.2    Gey, C.3    Heyraud, A.4    Zeikus, J.G.5    Henrissat, B.6
  • 40
    • 0031809938 scopus 로고    scopus 로고
    • Purification and properties of recombinant beta-galactosidase from Bacillus circulans
    • Fujimoto H., Miyasato M., Ito Y., Sasaki T., Ajisaka K. Purification and properties of recombinant beta-galactosidase from Bacillus circulans. Glycoconj. J. 15:1998;155-160.
    • (1998) Glycoconj. J. , vol.15 , pp. 155-160
    • Fujimoto, H.1    Miyasato, M.2    Ito, Y.3    Sasaki, T.4    Ajisaka, K.5
  • 41
    • 0034943702 scopus 로고    scopus 로고
    • Rapid screening of the aglycone specificity of glycosidases: Applications to enzymatic synthesis of oligosaccharides
    • Blanchard J.E., Withers S.G. Rapid screening of the aglycone specificity of glycosidases. applications to enzymatic synthesis of oligosaccharides Chem. Biol. 8:2001;627-633.
    • (2001) Chem. Biol. , vol.8 , pp. 627-633
    • Blanchard, J.E.1    Withers, S.G.2
  • 42
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene. 77:1989;51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 43
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi R., Krummel B., Saiki R.K. A general method of in vitro preparation and specific mutagenesis of DNA fragments. study of protein and DNA interactions Nucleic Acids Res. 16:1988;7351-7367.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 45
    • 0022017443 scopus 로고
    • Transformation of Aspergillus niger by the amdS gene of Aspergillus nidulans
    • Kelly J.M., Hynes M.J. Transformation of Aspergillus niger by the amdS gene of Aspergillus nidulans. EMBO J. 4:1985;475-479.
    • (1985) EMBO J. , vol.4 , pp. 475-479
    • Kelly, J.M.1    Hynes, M.J.2
  • 47
    • 0027686844 scopus 로고
    • Facile synthesis of acetylated glycosyl fluorides derived from di- and tri-saccharides
    • Jünnemann J., Thiem J., Pedersen C. Facile synthesis of acetylated glycosyl fluorides derived from di- and tri-saccharides. Carbohydr. Res. 249:1993;91-94.
    • (1993) Carbohydr. Res. , vol.249 , pp. 91-94
    • Jünnemann, J.1    Thiem, J.2    Pedersen, C.3
  • 49
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 50
    • 0028103275 scopus 로고
    • The CCP4 (Collaborative Computational Project Number 4) suite: Programs for protein crystallography
    • CCP4 The CCP4 (Collaborative Computational Project Number 4) suite. programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 51
    • 0026597444 scopus 로고
    • Free R-value: A novel statistical quantity for assessing the accuracy of crystal-structures
    • Brünger A.T. Free R-value. a novel statistical quantity for assessing the accuracy of crystal-structures Nature. 355:1992;472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 52
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D. 53:1997;240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 54
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf R.M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D. 55:1999;938-940.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.