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Biosci Biotechnol Biochem. 1995 Mar;59(3):459-63.

Chemical modification and amino acid sequence of active site in sugar beet alpha-glucosidase.

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Faculty of Agriculture, Hokkaido University, Sapporo, Japan.


The modification of amino acid residues in sugar beet alpha-glucosidase with conduritol B epoxide (CBE), an affinity labeling reagent, inactivated the enzyme. The inactivation followed pseudo-first-order kinetics. The enzyme was protected from inactivation by a competitive inhibitor, Tris, and the partially inactivated enzymes showed only the decrease of V values and no change in Km value. An 3H-CBE labeled peptide isolated from the digest of the inactivated enzyme with Lys-C protease was sequenced. The -COO- group of Asp was found to be specifically labeled, implicating that it is a catalytic group of the enzyme. The sequence around the essential Asp was determined to be -DGIWIDMNE-, which showed a high homology with those of other alpha-glucosidases.

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