Modulation of substrate preference of Thermus maltogenic amylase by mutation of the residues at the interface of a dimer
Citation
Park, S.-H., Kang, H.-K., Shim, J.-H., Woo, E.-J., Hong, J.-S., Kim, J.-W., Oh, B.-H., Lee, B.-H., Cha, H., and Park, K.-H. (2007). "Modulation of substrate preference of Thermus maltogenic amylase by mutation of the residues at the interface of a dimer.", Bioscience, Biotechnology, and Biochemistry (BBB), 71(6), pp. 1564-1567. doi : 10.1271/bbb.70017
Abstract
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 kcat/Km 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.