The distribution of carbohydrate side chains along the polypeptide chain of glucoamylase |
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Authors: | John H. Pazur Belin Liu Steven Pyke Craig R. Baumrucker |
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Affiliation: | (1) Paul M. Althouse Laboratory, Pennsylvania State University, 16802 University Park, Pennsylvania, USA;(2) Department of Dairy and Animal Science, Pennsylvania State University, University Park, USA |
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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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Keywords: | glucoamylase glycoprotein structure o-glycosidic linkage cyanogen bromide cleavage distribution of carbohydrates |
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