• Title of article

    Carbohydrate esterase family 4 enzymes: substrate specificity

  • Author/Authors

    Frederic Caufrier، نويسنده , , Aggeliki Martinou، نويسنده , , Claude Dupont، نويسنده , , Vassilis Bouriotis، نويسنده ,

  • Issue Information
    دوهفته نامه با شماره پیاپی سال 2003
  • Pages
    6
  • From page
    687
  • To page
    692
  • Abstract
    The substrate specificity of selected enzymes classified under Carbohydrate Esterase family 4 (CE4) has been examined. Chitin deacetylase from Mucor rouxii and both a native and a truncated form of acetyl xylan esterase from Streptomyces lividans were found to be active on both xylan and several soluble chitinous substrates. Furthermore, the activities of all enzymes examined were significantly increased in the presence of Co2+ when chitinous substrates were employed. However, the presence of this metal ion did not result in enhancing the activities of the enzymes when xylan was used as substrate. An acetyl xylan esterase from Bacillus pumilus, classified under Carbohydrate Esterase family 7, was found to be inactive towards all chitinous substrates tested. Finally, all enzymes examined were inactive towards cell wall peptidoglycan.
  • Keywords
    Chitin , Acetyl xylan esterase , Peptidoglycan , Xylan , Chitin deacetylase
  • Journal title
    Carbohydrate Research
  • Serial Year
    2003
  • Journal title
    Carbohydrate Research
  • Record number

    963693