Investigation of the Active Site of Human Salivary α-Amylase from the Modes of Action on Modified Maltooligosaccharides

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Abstract
The modes of action of two isozymes of human salivary α-amylase on phenyl α maltopentaoside, phenyl α-maltotetraoside, and their derivatives which have an iodo or an amino or a carboxyl group at their first or penultimate glucopyranosyl residues from the non-reducing-end were examined. It is conceivable that the active site of this enzyme is composed of tandem subsites (S4, S3, S2, S1′, S2′, and S3′) geometrically complementary to several glucose residues, and that the glucosidic bonds of the substrates are split between S1 and S1′. Product analysis of each digest strongly suggested the presence of a hydrophobic amino acid residue at subsite S3 in the active site of the enzyme. No difference in the modes of action on the substrates was found between the two isozymes, indicating that the three-dimensional structures of their active site areas are, at the least, similar.