T. Oyama et al., PROPERTY OF TAKA-AMYLASE-A WITH GLU OR ASP OF THE CATALYTIC RESIDUE REPLACED BY THE CORRESPONDING AMINE, Bioscience, biotechnology, and biochemistry, 60(8), 1996, pp. 1351-1352
Compared with the enzyme activity of a recombinant Taka-amylase A (wil
d TAA) at 25 degrees C and pH 5.3, those of two mutants (E230Q and D29
7N) were 1/10,000 and 1/16,000 for amylase activity, and 1/920 and les
s than 1/20,000 for maltosidase activity, respectively. This indicates
that all residual activities of E230Q are not due to contamination by
wild-type TAA. The results from difference spectroscopy suggested tha
t E230Q retains amylose binding ability.