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The NH2-terminal sequence (25 residues) of amphiphilic single polypeptide chain maltase-glucoamylase (EC 3.2.1.20) was determined by gas-phase sequencing. The result indicates that the NH2-terminal segment anchors the enzyme to the microvillar membrane. The single-chain form and the proteolytically processed two-chain form have two distinct active sites differing in heat stability. However, both sites are sensitive to chonduritol B-epoxide and have similar substrate specificity. The amphiphilic single-chain maltase-glucoamylase and the amphiphilic proteolytically processed form were inserted into liposomes and studied by electron microscopy. The results showed that the enzyme is predominantly present as a homodimeric complex in the membrane.
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