Putative exposed aromatic and hydroxyl residues on the surface of the N-terminal domains of Chi1 from Aeromonas caviae CB101 are essential for chitin binding and hydrolysis

Appl Environ Microbiol. 2005 Nov;71(11):7559-61. doi: 10.1128/AEM.71.11.7559-7561.2005.

Abstract

Chitinase Chi1 of Aeromonas caviae CB101 possesses chitin binding sites at both its N and C termini. Four putative exposed residues aligned in a line on the surface of the N-terminal domains of Chi1 were found to contribute to the enzyme-chitin binding and hydrolysis via site-directed mutagenesis. Also, it was found that Chi1 requires the cooperation of the N- and C-terminal domains to bind fully with crystalline and colloidal chitin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aeromonas / enzymology*
  • Aeromonas / genetics
  • Chitin / metabolism*
  • Chitinases / chemistry*
  • Chitinases / genetics
  • Chitinases / metabolism*
  • Hydrolysis
  • Hydroxyl Radical
  • Mutagenesis, Site-Directed
  • Structure-Activity Relationship

Substances

  • Chitin
  • Hydroxyl Radical
  • Chitinases