Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 71, Issue 6, Pages 1564-1567Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.70017
Keywords
amylopectin; amylose; cyclodextrin-degrading enzyme; mutagenesis; Thermus sp maltogenic amylase (ThMA)
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To elucidate the relationship between the substrate size and geometric shape of the catalytic site of Thermus maltogenic amylase, Gly50, Asp109, and Val431, located at the interface of the dimer, were replaced with bulky amino acids. The k(cat)/K-m value of the mutant for amylose increased significantly, whereas that for amylopectin decreased as compared to that of the wild-type enzyme. Thus, the substituted bulky amino acid residues modified the shape of the catalytic site, such that the ability of the enzyme to distinguish between small and large molecules like amylose and amylopectin was enhanced.
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