SEARCH

SEARCH BY CITATION

References

  • 1
    Coutinho, P.M. & Henrissat, B. (1999) Carbohydrate-active enzymes: an integrated database approach. In ‘Recent Advances in Carbohydrate Bioengineering’ (Gilbert, H.J., Davies, G., Henrissat, B. & SvenssonB., eds), pp. 312. The Royal Society of Chemistry, Cambridge.
  • 2
    Davies, G. & Henrissat, B. (1995) Structures and mechanisms of glycosyl hydrolases. Structure 3, 853859.
  • 3
    Street, I.P., Kempton, J.B. & 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, 99709978.
  • 4
    Whiters, S.G., Ruptiz, K., Trimbur, D. & Warren, R.A. (1992) Mechanistic consequence of mutation of the active site nucleophile glu 358 in Agrobacteriumβ-glucosidase. Biochemistry 31, 99799985.
  • 5
    Keresztessy, Z., Kiss, L. & Hughes, M.A. (1994) Investigation of the active site of the cyanogenic β-d-glucosidase (linamarase) from Manihot esculenta Crantz (cassava). I. Evidence for an essential carboxylate and a reactie histidine residue in a single catalytic center. Arch. Biochem. Biophys. 314, 142152.
  • 6
    Wang, Q., Trimbur, D., Graham, R., Warren, R.A.J. & Withers, S.G. (1995) Identification of the acid/base catalyst in Agrobacterium faecalisβ-glucosidase by kinetic analysis of mutants. Biochemistry 34, 1455414562.
  • 7
    Skoubas, A. & Georgatsos, J.G. (1997) Identification of essential amino acids for the catatytic activity of barley β-glucosidase. Phytochemistry 46, 9971003.
  • 8
    McIntosh, L.P., Hand, G., Johnson, P.E., Joshi, M.D., Körner, M., Plesniak, L.A., Ziser, L., Wakarchuk, W.W. & Withers, S.G. (1996) The pKa of the general acid/base carboxyl group of a glycosidase cycles during catalysis: a 13C-NMR study of Bacillus circulans xylanase. Biochemistry 35, 99589966.
  • 9
    Marana, S.R., Jacobs-Lorena, M., Terra, W.R. & Ferreira, C. (2001) Amino acid residues involved in substrate binding and catalysis in an insect digestive β-glycosidase. Biochim. Biophys. Acta 1545, 4152.
  • 10
    Burmeister, W.P., Cottaz, S., Driguez, H., Iori, R., Palmieri, S. & Henrissat, B. (1997) The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase. Structure 15, 663675.
  • 11
    Barrett, T., Suresh, C.G., Tolley, S.P., Dodson, E.J. & Hughes, M.A. (1995) The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase. Structure 3, 951960.
  • 12
    Sanz-Aparicio, J., Hermoso, J.A., Martínez-Ripoll, M., Lequerica, J.L. & Polaina, J. (1998) Cristal structure of β-glucosidase A from Bacillus polymyxa: Insights into the catalytic activity in family 1 glycosyl hydrolases. J. Mol. Biol. 275, 491502.
  • 13
    Aguilar, C.F., Sanderson, I., Moracci, M., Ciaramella, M., Nucci, R., Rossi, M. & Pearl, L.H. (1997) Crystal structure of the β-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: Resilence as a key factor in thermostability. J. Mol. Biol. 271, 789802.
  • 14
    Gebler, J.C., Trimbur, D.E., Warren, A.J., Aebersold, R., Namchuk, M. & Withers, S.G. (1995) Substrate-induced inactivation of a crippled β-glucosidase mutant: identification of the labeled amino acid and mutagenic analysis of its role. Biochemistry 34, 1454714533.
  • 15
    Tabor, S. & Richardson, C.C. (1985) A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA 82, 10741078.
  • 16
    Takashi, Y., Kanei-Ishii, C., Maekava, T., Fujimoto, J., Yamamoto, T. & Ishii, S. (1995) Increase of solubility of foregein proteins in Escherichia coli by co-production of the bacterial thioredoxin. J. Biol. Chem. 270, 2532825331.
  • 17
    Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680685.
  • 18
    Terra, W.R., Ferreira, C. & Bianchi, A.G. (1979) Distribution of digestive enzymes among the endo and ectoperithophic spaces and midgut cells of Rhynchosciara americana and its physiological significance. J. Insect Physiol. 25, 487494.
  • 19
    Blum, H., Beir, H. & Gross, H. (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8, 9399.
  • 20
    Gill, S.C. & von Hippel, P.H. (1989) Calculation of proteins extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319326.
  • 21
    Marana, S.R., Terra, W.R. & Ferreira, C. (2000) Purification and properties of a β-glycosidase purified from midgut cells of Spodoptera frugiperda (Lepidoptera) larvae. Insect Biochem. Mol. Biol. 30, 11391146.
  • 22
    Baker, J.E. & Woo, S.M. (1992) β-glucosidases in the rice weevil, Sitophilus oryzae: purification, properties, and activity levels in wheat-and legume feeding strains. Insect Biochem. Mol. Biol. 22, 495504.
  • 23
    Takahashi, K. (1968) The reaction of phenylglyoxal with arginine residues in proteins. J. Biol. Chem. 243, 61716179.
  • 24
    Yamasaki, R.B., Vega, A. & Feeney, R.E. (1980) Modification of available arginine residues in proteins by p-hydroxyphenylglyoxal. Anal. Biochem. 109, 3240.
  • 25
    Segel, H.I. (1993) Enzyme Kinetics. Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems. John Wiley & Sons, New York.
  • 26
    Guex, N. & Peitsch, M.C. (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling. Electrophoresis 18, 27142723.
  • 27
    Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F. & Higgins, D.G. (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 48764882.
  • 28
    Ippolito, J.A., Alexander, R.S. & Christianson, D.W. (1990) Hydrogen bond stereochemistry in protein structure and function. J. Mol. Biol. 215, 457471.
  • 29
    Joshi, M.D., Sidhu, G., Nielsen, J.E., Brayer, G.D., Withers, S.G. & McIntosh, L.P. (2001) Dissecting the eletrostatic interactions and pH-dependent activity of a family 11 glycosidase. Biochemistry 40, 1011510139.