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Original Articles

α-Glucosidase Mutant Catalyzes “α-Glycosynthase”-type Reaction

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Pages 928-933 | Received 26 Nov 2001, Accepted 20 Dec 2001, Published online: 22 May 2014

  • 1) Wang, Q., Graham, R. W., Trimbur, D., Warren, R. A. J., and Withers, S. G., Changing enzymatic reaction mechanisms by mutagenesis: conversion of a retaining glucosidase to an inverting enzyme. J. Am. Chem. Soc., 116, 11594-11595 (1994).
  • 2) Mackenzie, L. F., Wang, Q., Warren, R. A. J., and Withers, S. G., Glycosynthases: mutant glycosidases for oligosaccharide synthesis. J. Am. Chem. Soc., 120, 5583-5584 (1998).
  • 3) Mayer, C., Zechel, D. L., Reid, S. P., Warren, R. A. J., and Withers, S. G., The E358S mutant of Agrobacterium sp. β-glucosidase is a greatly improved glycosynthase. FEBS Lett., 466, 40-44 (2000).
  • 4) Trincone, A., Perugino, G., Rossi, M., and Moracci, M., A novel thermophilic glycosynthase that effects branching glycosylation. Bioorg. Med. Chem. Lett., 10, 365-368 (2000).
  • 5) Malet, C. and Planas, A., From β-glucanase to β-glucansynthase: glycosyl transfer to α-glycosyl fluorides catalyzed by a mutant endoglucanase lacking its catalytic nucleophile. FEBS Lett., 440, 208-212 (1998).
  • 6) Chiba, S., Molecular mechanism in α-glucosidase and glucoamylase. Biosci. Biotechnol. Biochem., 61, 1233-1239 (1997).
  • 7) Okuyama, M., Okuno, A., Shimizu, N., Mori, H., Kimura, A., and Chiba, S., Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of α-glucosidase from Schizosaccharomyces pombe. Eur. J. Biochem., 268, 2270-2280 (2001).
  • 8) Kimura, A., Takata, M., Fukushi, Y., Mori, H., Matsui, H., and Chiba, S., A catalytic amino acid and primary structure of active site in Aspergillus niger α-glucosidase. Biosci. Biotechnol. Biochem., 61, 1091-1098 (1997).
  • 9) Datta, A. K., Efficient amplification using ‘megaprimer’ by asymmetric polymerase chain reaction. Nucleic Acids Res., 23, 4530-4531 (1995).
  • 10) Chiba, S. and Shimomura, T., Comparative biochemical studies on α-glucosidases: part III. Transglucosidation action of an α-glucosidase from Schizosaccharomyces pombe. Agric. Biol. Chem., 30, 536-540 (1966).
  • 11) Kitahata, S., Brewer, C. F., Genghof, D. S., Sawai, T., and Hehre, E. J., Scope and mechanism of carbohydrase action. Stereocomplementary hydrolytic and glucosyl-transferring actions of glucoamylase and glucodextranase with α- and β-D-glucosyl fluoride. J. Biol. Chem., 256, 6017-6026 (1981).
  • 12) Hehre, E. J., Sawai, T., Brewer, C. F., Nakano, M., and Kanda, T., Trehalase: stereocomplementary hydrolytic and glucosyl transfer reactions with α- and β-D-glucosyl fluoride. Biochemistry, 21, 3090-3097 (1982).
  • 13) Hehre, E. J., Brewer, C. F., and Genghof, D. S., Scope and mechanism of carbohydrase action. Hydrolytic and nonhydrolytic actions of β-amylase on α- and β-maltosyl fluoride. J. Biol. Chem., 254, 5942-5950 (1979).
  • 14) Hehre, E. J., Okada, G., and Genghof, D. S., Configurational specificity: unappreciated key to understanding enzymic reversions and de novo glycosidic bond synthesis. I. Reversal of hydrolysis by α-, β- and glucoamylases with donors of correct anomeric form. Arch. Biochem. Biophys., 135, 75-89 (1969).
  • 15) Okada, G., Genghof, D. S., and Hehre, E. J., Reversion and transglycosylation by amylases. J. Jpn. Soc. Starch Sci., 25, 113-123 (1978).
  • 16) Hehre, E. J., Okada, G., and Genghof, D. S., Glycosylation as the paradigm of carbohydrase action: evidence from the actions of amylases. Advan. Chem. Ser., 117, 309-333 (1973).
  • 17) Chiba, S., Kimura, A., and Matsui, H., Quantitative study of anomeric forms of glucose produced by α-glucosidases and glucoamylases. Agric. Biol. Chem., 47, 1741-1746 (1983).
  • 18) Kimura, A. and Chiba, S., Quantitative study of anomeric forms of maltose produced by α- and β-amylases. Agric. Biol. Chem., 47, 1747-1753 (1983).
  • 19) Takayanagi, T., Okada, G., and Chiba, S., Quantitative study of anomeric forms of isomaltose and glucose produced by isomalto-dextranase and glucodextranase. Agric. Biol. Chem., 51, 2237-2341 (1987).
  • 20) Lee, J.-H., Tsuji, M., Nakamura, M., Nishimoto, M., Okuyama, M., Mori, H., Kimura, A., Matsui, H., and Chiba, S., Purification and identification of essential ionizable groups of honeybee, Apis mellifera L., trehalase. Biosci. Biotechnol. Biochem., 65, 2657-2665 (2001).

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