Site-directed mutagenesis of the Asp-197 and Asp-202 residues in chitinase A1 of Bacillus circulans WL-12.
The contribution of the Asp-197 and Asp-202 residues in chitinase A1 of Bacillus circulans WL-12 to the catalytic reaction was studied by site-directed mutagenesis of these residues. A kinetic analysis of the purified mutant chitinases suggests the involvement of both the Asp-197 and Asp-202 residues in the catalytic events of this enzyme, although the effects of mutations of Asp-197 were less severe than those of the other mutations.
Watanabe
T
T
Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University, Japan.
Uchida
M
M
Kobori
K
K
Tanaka
H
H
D000595:Amino Acid Sequence; D001224:Aspartic Acid / Q000378:metabolism*; D001407:Bacillus / Q000201:enzymology* / Q000235:genetics; D001483:Base Sequence; D002384:Catalysis; D002688:Chitinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009838:Oligodeoxyribonucleotides; D017386:Sequence Homology, Amino Acid
D009838:Oligodeoxyribonucleotides; D001224:Aspartic Acid; D002688:Chitinases