Abstract
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.
MeSH terms
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Amino Acid Sequence
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Aspartic Acid / metabolism*
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Bacillus / enzymology*
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Bacillus / genetics
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Base Sequence
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Catalysis
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Chitinases / chemistry
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Chitinases / genetics
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Chitinases / metabolism*
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Kinetics
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Oligodeoxyribonucleotides
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Sequence Homology, Amino Acid
Substances
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Oligodeoxyribonucleotides
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Aspartic Acid
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Chitinases
Associated data
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GENBANK/D12647
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GENBANK/D14536
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GENBANK/L14614
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GENBANK/M80793
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GENBANK/X71080
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SWISSPROT/P29024
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SWISSPROT/P29025
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SWISSPROT/P29027
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SWISSPROT/P29029
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SWISSPROT/P29030
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SWISSPROT/P32470