Site-directed Mutagenesis of the Asp-197 and Asp-202 Residues in Chitinase A1 of Bacillus Circulans WL-12

Biosci Biotechnol Biochem. 1994 Dec;58(12):2283-5. doi: 10.1271/bbb.58.2283.

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

  • Amino Acid Sequence
  • Aspartic Acid / metabolism*
  • Bacillus / enzymology*
  • Bacillus / genetics
  • Base Sequence
  • Catalysis
  • Chitinases / chemistry
  • Chitinases / genetics
  • Chitinases / metabolism*
  • Kinetics
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Oligodeoxyribonucleotides
  • Sequence Homology, Amino Acid

Substances

  • Oligodeoxyribonucleotides
  • Aspartic Acid
  • Chitinases

Associated data

  • GENBANK/D12647
  • GENBANK/D14536
  • GENBANK/L14614
  • GENBANK/M80793
  • GENBANK/X71080
  • SWISSPROT/P29024
  • SWISSPROT/P29025
  • SWISSPROT/P29027
  • SWISSPROT/P29029
  • SWISSPROT/P29030
  • SWISSPROT/P32470