Studies on the Substrate Specificity of Taka-amylase A

Publisher Website
Google Scholar
Abstract
Several specimens of a mixture of partially O-methylated derivatives of phenyl α-maltoside were prepared where O-methylated glucose residues were predominantly mono-O-methyl derivative. The enzymatic action of Taka-amylase A [EC 3. 2. 1. 1] on these specimens was investigated, and the reaction products were detected. Among the reaction products, the following maltose derivatives were identified: 3′-O-methyl-maltose, 4′-O-methyl-maltose, 6′-O-methyl-maltose, and 4′, 6′-di-O-methyl-maltose. Any maltose derivative which had O-methyl substituent on the reducing end glucose residue was never produced by the enzyme. Phenyl 2′-O-methyl-α-maltoside which was inferred to be present in a specimen, was found to be resistant to the enzymatic action. Consequently, it seemed that in the maltose moiety of a substrate molecule all the hydroxyls on the reducing end glucose residue and the 2-hydroxyl on the non-reducing end residue played important roles in the enzymatic reaction.

This publication has 0 references indexed in Scilit: