메뉴 건너뛰기




Volumn 21, Issue 4-5, 2003, Pages 223-231

Unusual role of the 2-OH group of oligosaccharide substrates in the mechanism of Bacillus 1,3-1,4-β-glucanase

Author keywords

2 deoxyglycoside; Glycosidase; Mechanism; Non covalent interactions; Ring distortion

Indexed keywords

BIOCATALYSTS; ENZYMES; HYDROGEN BONDS; OLIGOMERS; OPTIMIZATION;

EID: 0347337761     PISSN: 10242422     EISSN: None     Source Type: Journal    
DOI: 10.1080/10242420310001618500     Document Type: Conference Paper
Times cited : (2)

References (48)
  • 2
    • 0029684150 scopus 로고    scopus 로고
    • Site-directed mutagenesis using double-stranded plasmid DNA templates
    • Braman, J., Papworth, C. and Greener, A. (1996) "Site-directed mutagenesis using double-stranded plasmid DNA templates", Methods Mol. Biol. 57, 31-44.
    • (1996) Methods Mol. Biol. , vol.57 , pp. 31-44
    • Braman, J.1    Papworth, C.2    Greener, A.3
  • 3
    • 0032557232 scopus 로고    scopus 로고
    • Substrate distortion to a boat conformation at subsite - 1 is critical in the mechanism of family 18 chitinases
    • Brameld, K.A. and Goddard III, W.A. (1998) "Substrate distortion to a boat conformation at subsite - 1 is critical in the mechanism of family 18 chitinases", J. Am. Chem. Soc. 120, 3571-3580.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3571-3580
    • Brameld, K.A.1    Goddard III, W.A.2
  • 4
    • 0038562120 scopus 로고    scopus 로고
    • A large difference in the thermodynamics in binding of isofagomine and 1-deoxynojirimycin to β-glucosidase
    • Bülow, A., Plesner, I.W. and Bols, M. (2000) "A large difference in the thermodynamics in binding of isofagomine and 1-deoxynojirimycin to β-glucosidase", J. Am. Chem. Soc. 122, 8567-8568.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8567-8568
    • Bülow, A.1    Plesner, I.W.2    Bols, M.3
  • 6
  • 7
    • 0026668499 scopus 로고
    • Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) β-galactosidase from Escherichia coli
    • Gebler, J.C., Aebersold, R. and Withers, S.G. (1992) "Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) β-galactosidase from Escherichia coli", J. Biol. Chem. 267, 11126-11130.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11126-11130
    • Gebler, J.C.1    Aebersold, R.2    Withers, S.G.3
  • 8
    • 0029115396 scopus 로고
    • Crystal and molecular structure at 0.16 nm resolution of the hybrid Bacillus endo-1,3-1,4-β-D-glucan 4-glucanohydrolase H(A16-M)
    • Hahn, M., Keitel, T. and Heinemann, U. (1995b) "Crystal and molecular structure at 0.16 nm resolution of the hybrid Bacillus endo-1,3-1,4-β-D-glucan 4-glucanohydrolase H(A16-M)", Eur. J. Biochem. 232, 849-859.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 849-859
    • Hahn, M.1    Keitel, T.2    Heinemann, U.3
  • 9
    • 0028841188 scopus 로고
    • Crystal structure of Bacillus licheniformis 1,3-1,4-β-D-glucan 4-glucanohydrolase at 1.8Å resolution
    • Hahn, M., Pons, J., Planas, A., Querol, E. and Heinemann, U. (1995a) "Crystal structure of Bacillus licheniformis 1,3-1,4-β-D-glucan 4-glucanohydrolase at 1.8Å resolution", FEBS Lett. 374, 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
  • 10
    • 0030819176 scopus 로고    scopus 로고
    • Assignment of sweet almond β-glucosidase as a family 1 glycosidase and identification of its active site nucleophile
    • He, S.M. and Withers, S.G. (1997) "Assignment of sweet almond β-glucosidase as a family 1 glycosidase and identification of its active site nucleophile", J. Biol. Chem. 272, 24864-24867.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24864-24867
    • He, S.M.1    Withers, S.G.2
  • 11
    • 0029805094 scopus 로고    scopus 로고
    • Enzymology and folding of natural and engineered bacterial β-glucanases studied by X-ray crystallography
    • Heinemann, U., Aÿ, J., Gaiser, O., Müller, J.J. and Ponnuswamy, M.N. (1996) "Enzymology and folding of natural and engineered bacterial β-glucanases studied by X-ray crystallography", Biol. Chem. 377, 447-454.
    • (1996) Biol. Chem. , vol.377 , pp. 447-454
    • Heinemann, U.1    Aÿ, J.2    Gaiser, O.3    Müller, J.J.4    Ponnuswamy, M.N.5
  • 12
    • 0028225393 scopus 로고
    • Identification of active site carboxylic residues in Bacillus licheniformis 1,3-1,4-β-D-glucan 4-glucanohydrolase by site-directed mutagenesis
    • Juncosa, M., Pons, J., Dot, T., Querol, E. and Planas, A. (1994) "Identification of active site carboxylic residues in Bacillus licheniformis 1,3-1,4-β-D-glucan 4-glucanohydrolase by site-directed mutagenesis", J. Biol. Chem. 269, 14530-14535.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14530-14535
    • Juncosa, M.1    Pons, J.2    Dot, T.3    Querol, E.4    Planas, A.5
  • 13
    • 0027161796 scopus 로고
    • Molecular and active-site structure of a Bacillus 1,3-1,4-β-glucanase
    • Keitel, T., Simon, O., Borriss, R. and Heinemann, U. (1993) "Molecular and active-site structure of a Bacillus 1,3-1,4-β-glucanase", Proc. Natl. Acad. Sci. USA 90, 5287-5291.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5287-5291
    • Keitel, T.1    Simon, O.2    Borriss, R.3    Heinemann, U.4
  • 14
    • 0026803010 scopus 로고
    • Mechanism of Agrobacterium β-glucosidase: Kinetic studies
    • Kempton, J.B. and Withers, S.G. (1992) "Mechanism of Agrobacterium β-glucosidase: Kinetic studies", Biochemistry 31, 9961-9969.
    • (1992) Biochemistry , vol.31 , pp. 9961-9969
    • Kempton, J.B.1    Withers, S.G.2
  • 15
    • 84979146389 scopus 로고
    • Stereochemistry and the mechanism of enzymatic reaction
    • Koshland, D.E. Jr. (1953) "Stereochemistry and the mechanism of enzymatic reaction", Biol. Rev. 28, 416-436.
    • (1953) Biol. Rev. , vol.28 , pp. 416-436
    • Koshland Jr., D.E.1
  • 16
    • 0034741146 scopus 로고    scopus 로고
    • Noeuromycin, a glycosyl cation mimic that strongly inhibits glycosidases
    • Liu, H., Liang, X., Sohoel, H., Bülow, A. and Bols, M. (2001) "Noeuromycin, a glycosyl cation mimic that strongly inhibits glycosidases", J. Am. Chem. Soc. 123, 5116-5117.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5116-5117
    • Liu, H.1    Liang, X.2    Sohoel, H.3    Bülow, A.4    Bols, M.5
  • 17
    • 0027772710 scopus 로고
    • Stereochemical course and structure of the products of the enzymatic action of endo-1,3-1,4-β-D-glucan 4-glucanohydrolase from Bacillus licheniformis
    • Malet, C., Jiménez-Barbero, J., Bernabé, M., Brosa, C. and Planas, A. (1993) "Stereochemical course and structure of the products of the enzymatic action of endo-1,3-1,4-β-D-glucan 4-glucanohydrolase from Bacillus licheniformis", Biochem. J. 296, 753-758.
    • (1993) Biochem. J. , vol.296 , pp. 753-758
    • Malet, C.1    Jiménez-Barbero, J.2    Bernabé, M.3    Brosa, C.4    Planas, A.5
  • 18
    • 0030694040 scopus 로고    scopus 로고
    • Mechanism of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases: Kinetics and pH studies with 4-methylumbelliferyl β-glucan oligosaccharides
    • Malet, C. and Planas, A. (1997) "Mechanism of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases: Kinetics and pH studies with 4-methylumbelliferyl β-glucan oligosaccharides", Biochemistry 36, 13838-13848.
    • (1997) Biochemistry , vol.36 , pp. 13838-13848
    • Malet, C.1    Planas, A.2
  • 19
    • 0029082880 scopus 로고
    • Synthesis of 4-methylumbelliferyl-β-D-glucan oligosaccharides as specific chromophoric substrates of (1 → 3,1 → 4)-β-D-glucan 4-glucanohydrolases
    • Malet, C., Viladot, J.L., Ochoa, A., Gállego, B., Brosa, C. and Planas, A. (1995) "Synthesis of 4-methylumbelliferyl-β-D-glucan oligosaccharides as specific chromophoric substrates of (1 → 3,1 → 4)-β-D-glucan 4-glucanohydrolases", Carbohydr. Res. 274, 285-301.
    • (1995) Carbohydr. Res. , vol.274 , pp. 285-301
    • Malet, C.1    Viladot, J.L.2    Ochoa, A.3    Gállego, B.4    Brosa, C.5    Planas, A.6
  • 20
    • 0026666602 scopus 로고
    • Binding energy and catalysis. Fluorinated and deoxygenated glycosides as mechanistic probes of Escherichia coli (lac Z) β-galactosidase
    • McCarter, J.D., Adam, M.J. and Withers, S.G. (1992) "Binding energy and catalysis. Fluorinated and deoxygenated glycosides as mechanistic probes of Escherichia coli (lac Z) β-galactosidase", Biochem. J. 286, 721-727.
    • (1992) Biochem. J. , vol.286 , pp. 721-727
    • McCarter, J.D.1    Adam, M.J.2    Withers, S.G.3
  • 21
    • 0029666454 scopus 로고    scopus 로고
    • The pK(a) of the general acid/base carboxyl group of a glycosidase cycles during catalysis: A C-13-NMR study of Bacillus circulans xylanase
    • McIntosh, L.P., Hand, G., Johnson, P.E., Joshi, M.D., Korner, M., Plesniak, L.A., Ziser, L., Wakarchuk, W.W. and Withers, S.G. (1996) "The pK(a) of the general acid/base carboxyl group of a glycosidase cycles during catalysis: A C-13-NMR study of Bacillus circulans xylanase", Biochemistry 35, 9958-9966.
    • (1996) Biochemistry , vol.35 , pp. 9958-9966
    • McIntosh, L.P.1    Hand, G.2    Johnson, P.E.3    Joshi, M.D.4    Korner, M.5    Plesniak, L.A.6    Ziser, L.7    Wakarchuk, W.W.8    Withers, S.G.9
  • 22
    • 0020856703 scopus 로고
    • Energy of binding of Aspergillus oryzae β-glucosidase with the substrate, and the mechanism of its enzymic action
    • Mega, T. and Matsushima, Y. (1983) "Energy of binding of Aspergillus oryzae β-glucosidase with the substrate, and the mechanism of its enzymic action", J. Biochem. 94, 1637-1647.
    • (1983) J. Biochem. , vol.94 , pp. 1637-1647
    • Mega, T.1    Matsushima, Y.2
  • 23
    • 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. and Withers, S.G. (1994) "Identification of glutamic acid 78 as the active site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass spectrometry", Biochemistry 33, 7027-7032.
    • (1994) Biochemistry , vol.33 , pp. 7027-7032
    • Miao, S.1    Ziser, L.2    Aebersold, R.3    Withers, S.G.4
  • 25
    • 0034010063 scopus 로고    scopus 로고
    • A comparison of glucose- and glucosamine-related inhibitors: Probing the interactions of the 2-hydroxy group with retaining β-glucosidases
    • Panday, N., Meyyappan, M. and Vasella, A. (2000) "A comparison of glucose- and glucosamine-related inhibitors: Probing the interactions of the 2-hydroxy group with retaining β-glucosidases", Helv. Chim. Acta 83, 513-538.
    • (2000) Helv. Chim. Acta , vol.83 , pp. 513-538
    • Panday, N.1    Meyyappan, M.2    Vasella, A.3
  • 26
    • 0033534171 scopus 로고    scopus 로고
    • Protein-carbohydrate interactions defining substrate specificity in Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases as dissected by mutational analysis
    • Piotukh, K., Serra, V., Borriss, R. and Planas, A. (1999) "Protein-carbohydrate interactions defining substrate specificity in Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases as dissected by mutational analysis", Biochemistry 38, 16092-16104.
    • (1999) Biochemistry , vol.38 , pp. 16092-16104
    • Piotukh, K.1    Serra, V.2    Borriss, R.3    Planas, A.4
  • 27
    • 0034731485 scopus 로고    scopus 로고
    • Bacterial 1,3-1,4-β-glucanases: Structure, function and protein engineering
    • Planas, A. (2000) "Bacterial 1,3-1,4-β-glucanases: Structure, function and protein engineering", Biochim. Biophys. Acta 1543, 361-382.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 361-382
    • Planas, A.1
  • 28
    • 0031689979 scopus 로고    scopus 로고
    • Synthesis of aryl 3-O-β-cellobiosyl-β-D-glucopyranosides for reactivity studies of 1,3-1,4-β-glucanases
    • Planas, A., Abel, M., Millet, O., Palasí, J., Pallarés, C. and Viladot, J.Ll. (1998) "Synthesis of aryl 3-O-β-cellobiosyl-β-D-glucopyranosides for reactivity studies of 1,3-1,4-β-glucanases", Carbohydr. Res. 310, 53-64.
    • (1998) Carbohydr. Res. , vol.310 , pp. 53-64
    • Planas, A.1    Abel, M.2    Millet, O.3    Palasí, J.4    Pallarés, C.5    Viladot, J.Ll.6
  • 29
    • 0026612227 scopus 로고
    • Substrate specificity of small-intestinal lactase. Assessment of the role of the substrate hydroxyl groups
    • Rivera-Sagredo, A., Cañada, F.J., Nieto, O., Jiménez-Barbero, J. and Martin-Lomas, M. (1992) "Substrate specificity of small-intestinal lactase. Assessment of the role of the substrate hydroxyl groups", Eur. J. Biochem. 209, 415-422.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 415-422
    • Rivera-Sagredo, A.1    Cañada, F.J.2    Nieto, O.3    Jiménez-Barbero, J.4    Martin-Lomas, M.5
  • 30
    • 0019430979 scopus 로고
    • Role of sugar hydroxyl groups in glycosidase hydrolysis. Cleavage mechanis of deoxyglucosides and related substrates by β-glucosidase A3 from Aspergillus wentti
    • Roeser, K.R. and Legler, G. (1981) "Role of sugar hydroxyl groups in glycosidase hydrolysis. Cleavage mechanis of deoxyglucosides and related substrates by β-glucosidase A3 from Aspergillus wentti", Biochim. Biophys. Acta 657, 321-333.
    • (1981) Biochim. Biophys. Acta , vol.657 , pp. 321-333
    • Roeser, K.R.1    Legler, G.2
  • 31
    • 0019889069 scopus 로고
    • Oxygen-18 leaving group kinetic isotope effects on the hydrolysis of nitrophenyl glycosides. 2. Lysozyme and β-glucosidase: Acid and alkaline hydrolysis
    • Rosenberg, S. and Kirsch, J.F. (1981) "Oxygen-18 leaving group kinetic isotope effects on the hydrolysis of nitrophenyl glycosides. 2. Lysozyme and β-glucosidase: Acid and alkaline hydrolysis", Biochemistry 20, 3196-3204.
    • (1981) Biochemistry , vol.20 , pp. 3196-3204
    • Rosenberg, S.1    Kirsch, J.F.2
  • 33
    • 0033609135 scopus 로고    scopus 로고
    • Sugar ring distortion in the glycosyl - Enzyme intermediate of a family G/11 xylanase
    • Sidhu, G., Withers, S.G., Nguyen, N.T., McIntosh, L.P., Ziser L. and Brayer, G.D. (1999) "Sugar ring distortion in the glycosyl - Enzyme intermediate of a family G/11 xylanase", Biochemistry 38, 5346-5354.
    • (1999) Biochemistry , vol.38 , pp. 5346-5354
    • Sidhu, G.1    Withers, S.G.2    Nguyen, N.T.3    McIntosh, L.P.4    Ziser, L.5    Brayer, G.D.6
  • 34
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymic glycosyl transfer
    • Sinnott, M.L. (1990) "Catalytic mechanisms of enzymic glycosyl transfer", Chem. Rev. 90, 1171-1202.
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 35
    • 0015621418 scopus 로고
    • The mechanism of action of β-galactosidase. Effect of aglycone nature and α-deuterium substitution on the hydrolysis of aryl galactosides
    • Sinnott, M.L. and Souchard, I.J.L. (1973) "The mechanism of action of β-galactosidase. Effect of aglycone nature and α-deuterium substitution on the hydrolysis of aryl galactosides", Biochem. J. 133, 89-98.
    • (1973) Biochem. J. , vol.133 , pp. 89-98
    • Sinnott, M.L.1    Souchard, I.J.L.2
  • 36
    • 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. and Withers, S.G. (1992) "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, 9970-9978.
    • (1992) Biochemistry , vol.31 , pp. 9970-9978
    • Street, I.P.1    Kempton, J.B.2    Withers, S.G.3
  • 37
    • 0025778735 scopus 로고
    • Lysozyme revisited: Crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D
    • Strynadka, N.C.J. and James, M.N.G. (1991) "Lysozyme revisited: Crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D", J. Mol. Biol. 220, 401-424.
    • (1991) J. Mol. Biol. , vol.220 , pp. 401-424
    • Strynadka, N.C.J.1    James, M.N.G.2
  • 38
    • 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. and Davies, G.J. (1996) "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, 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
  • 39
    • 0033937325 scopus 로고    scopus 로고
    • Glycosidase-catalyzed hydrolysis of 2-deoxyglucopyranosyl pyridinium salts: Effect of the 2-OH group on binding and catalysis
    • Tanaka, K.S.E., Zhu, J., Huang, X., Lipari, F. and Bennet, A.J. (2000) "Glycosidase-catalyzed hydrolysis of 2-deoxyglucopyranosyl pyridinium salts: Effect of the 2-OH group on binding and catalysis", Can. J. Chem. 78, 577-582.
    • (2000) Can. J. Chem. , vol.78 , pp. 577-582
    • Tanaka, K.S.E.1    Zhu, J.2    Huang, X.3    Lipari, F.4    Bennet, A.J.5
  • 41
    • 0028224697 scopus 로고
    • Mechanisms of cellulases and xylanases: A detailed kinetic study of the exo-β-1,4-glycanase from Cellulomonas fimi
    • Tull, D. and Withers, S.G. (1994) "Mechanisms of cellulases and xylanases: A detailed kinetic study of the exo-β-1,4-glycanase from Cellulomonas fimi", Biochemistry 33, 6363-6370.
    • (1994) Biochemistry , vol.33 , pp. 6363-6370
    • Tull, D.1    Withers, S.G.2
  • 42
    • 0001263410 scopus 로고
    • Kinetic α-deuterium isotope effects for enzymic and acid hydrolysis of aryl-β-D-glycopyranosides
    • Van Doorslaer, E., Van Opstal, O., Kersters-Hilerson, H. and De Bruyne, C.K. (1984) "Kinetic α-deuterium isotope effects for enzymic and acid hydrolysis of aryl-β-D-glycopyranosides", Bioorg. Chem. 12, 158-169.
    • (1984) Bioorg. Chem. , vol.12 , pp. 158-169
    • Van Doorslaer, E.1    Van Opstal, O.2    Kersters-Hilerson, H.3    De Bruyne, C.K.4
  • 43
    • 0032508394 scopus 로고    scopus 로고
    • Probing the mechanism of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases by chemical rescue of inactive mutants at catalytically essential residues
    • Viladot, J.L., De Ramon, E., Durany, O. and Planas, A. (1998) "Probing the mechanism of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases by chemical rescue of inactive mutants at catalytically essential residues", Biochemistry 37, 11332-11342.
    • (1998) Biochemistry , vol.37 , pp. 11332-11342
    • Viladot, J.L.1    De Ramon, E.2    Durany, O.3    Planas, A.4
  • 44
    • 0035310774 scopus 로고    scopus 로고
    • Long-lived glycosyl - Enzyme intermediate mimic produced by formate re-activation of a mutant endoglucanase lacking its catalytic nucleophile
    • Viladot, J.L., Canals, F., Batllori, X. and Planas, A. (2001) "Long-lived glycosyl - Enzyme intermediate mimic produced by formate re-activation of a mutant endoglucanase lacking its catalytic nucleophile", Biochem. J. 355, 79-86.
    • (2001) Biochem. J. , vol.355 , pp. 79-86
    • Viladot, J.L.1    Canals, F.2    Batllori, X.3    Planas, A.4
  • 45
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lyzozyme proceeds via a covalent intermediate
    • Vocadlo, D.J., Davies, G.J., Laine, R. and Withers, S.G. (2001) "Catalysis by hen egg-white lyzozyme proceeds via a covalent intermediate", Nature 412, 835-838.
    • (2001) Nature , vol.412 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 46
    • 0034600322 scopus 로고    scopus 로고
    • A new, simple, high-affinity glycosidase inhibitor: Analysis of binding through X-ray crystallography, mutagenesis, and kinetic analysis
    • Williams, S.J., Notenboom, V., Wicki, J., Rose, D.R. and Withers, S.G. (2000) "A new, simple, high-affinity glycosidase inhibitor: Analysis of binding through X-ray crystallography, mutagenesis, and kinetic analysis", J. Am. Chem. Soc. 122, 4229-4230.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 4229-4230
    • Williams, S.J.1    Notenboom, V.2    Wicki, J.3    Rose, D.R.4    Withers, S.G.5
  • 47
    • 0035314098 scopus 로고    scopus 로고
    • Mechanism of glycosyl transferases and hydrolases
    • Withers, S.G. (2001) "Mechanism of glycosyl transferases and hydrolases", Carbohyd. Polym. 44, 325-337.
    • (2001) Carbohyd. Polym. , vol.44 , pp. 325-337
    • Withers, S.G.1
  • 48
    • 0001410590 scopus 로고
    • Identification of a covalent α-D-glucopyranosyl enzyme intermediate formed on a β-glucosidase
    • Withers, S.G. and Street, I.P. (1988) "Identification of a covalent α-D-glucopyranosyl enzyme intermediate formed on a β-glucosidase", J. Am. Chem. Soc. 110, 8551-8553.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 8551-8553
    • Withers, S.G.1    Street, I.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.