Abstract
Glucoamylase is a starch-hydrolyzing enzyme with a glycoprotein structure, used industrially for the conversion of starch to glucose, citric acid, corn syrups, and high-fructose sweeteners. This enzyme possesses an unusual type of structure in which many carbohydrate side chains are linked O-glycosidically to serine and threonine residues of the polypeptide chain. The carbohydrate side chains may be single monosaccharide residues or oligosaccharides of mannose, glucose, galactose, and in some cases N-acetylglucosamine. New data from experiments on the CNBr fragmentation of glucoamylase followed by chemical and immunological characterization of the fragments show that the carbohydrate side chains are distributed randomly along the polypeptide chain. Such a structure is appropriately termed a random model reprensentation for the glucoamylase molecule.
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References
Arnold, W. N. (1969). Biochim. Biophys. Acta 178, 347–353.
Boel, E., Hansen, M. T., Hjort, I., Høegh, I., and Fiil, N. P. (1984). The EMBO. J. 3, 1581–1585.
Coffey, J. W., and DeDuve, C. (1968). J. Biol. Chem. 243, 3255–3263.
Davis, B. J. (1964). Ann. N. Y. Acad. Sci. 121, 404–427.
Fairbanks, G., Steck, T. L., and Wallach, D. F. H. (1971). Biochemistry 10, 2606–2617.
Gum, E. K. Jr., and Brown, R. D. Jr. (1976). Biochim. Biophys. Acta. 446, 371–386.
Gunnarsson, A., Svensson, B., Nilsson, B., and Svensson, S. (1984). J. Biochem. 145, 463–467.
Innis, M. A., Holland, M. J., McCabe, P. C., Cole, G. E., Wittman, V. P., Tal, R., Watt, K. W. K., Gelfand, D. H., Holland, J. P., and Meade, H. J. (1985). Science 228, 21–26.
Langlois, D. P. (1953). Food. Tech. August, 303–306.
Lineback, D. R., and Aira, L. A. (1972). Cereal Chem. 49, 283–296.
Lineback, D. R., and Baumann, W. E. (1970). Carbohydrate Res. 14, 341–353.
MacAllister, R. V. (1979). Adv. Carbohydrate Chem. Biochem. 36, 15–56.
Manjunath, P., and Raghavendra Rao, M. R. (1980). Indian J. Biochem. Biophys. 17, 388–390.
Martin, R. G., and Ames, B. N. (1961). J. Biol. Chem. 236, 1372–1379.
Montreuil, J. (1980). Adv. Carbohydrate Chem. Biochem. 37, 157–223.
Ohnishi, M., Yamashita, T., and Hiromi, K. (1976) J. Biochem. 79, 1007–1012.
Pazur, J. H., and Aronson, N. N. Jr. (1972). Adv. Carbohydrate Chem. Biochem. 27, 301–341.
Pazur, J. H., and Kleppe, K. (1962). J. Biol. Chem. 237, 1002–1006.
Pazur, J. H., French, D., and Knapp, D. W. (1950). Proc. Iowa. Acad. Sci. 57, 203–209.
Pazur, J. H., Kleppe, K., and Anderson, J. S. (1962). Biochem. Biophys. Acta 65, 369–372.
Pazur, J. H., Kleppe, K., and Ball, E. M. (1963). Arch. Biochem. Biophys. 103, 515–518.
Pazur, J. H., Knull, H. R., and Simpson, D. L. (1970). Biochem. Biophys. Res. Commun. 40, 110–116.
Pazur, J. H., Knull, H. R., and Cepure, A. (1971). Carbohydrate Res. 20, 83–96.
Pazur, J. H., Tominaga, Y., Forsberg, L. S., and Simpson, D. L. (1980). Carbohydrate Res. 84, 103–114.
Pazur, J. H., Forry, K. R., Tominaga, Y., and Ball, E. M. (1981). Biochem. Biophys. Res. Commun. 100, 420–426.
Pazur, J. H., Tominaga, Y., and Kelly, S. (1984). J. Protein Chem. 3, 49–62.
Pazur, J. H., DeHoff, D. K., Miskiel, F. J., and Baumrucker, C. R. (1986). Carbohydrate Res. 149, 137–147.
Rosenthal, A. L., and Nordin, J. H. (1975). J. Biol. Chem. 256, 5295–5303.
Simon, J. P., Schorr, J. M., and Phillips, A. T. (1974). J. Biol. Chem. 249, 1993–1999.
Svensson, B., Pedersen, T. G., Svendsen, I., Sakai, T., and Ottensen, M. (1982). Carlsberg Res. Commun. 47, 55–69.
Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983). Carlsberg Res. Commun. 48, 529–544.
Svensson, B., Larsen, K., and Gunnarsson, A. (1986) Eur. J. Biochem. 154, 497–502.
Underkofler, L. A. (1969). Adv. Chem. Ser. 95, 343–358.
Weber, K., and Osborn, M. (1969). J. Biol. Chem. 244, 4406–4412.
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Pazur, J.H., Liu, B., Pyke, S. et al. The distribution of carbohydrate side chains along the polypeptide chain of glucoamylase. J Protein Chem 6, 517–527 (1987). https://doi.org/10.1007/BF00276737
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DOI: https://doi.org/10.1007/BF00276737