• Title of article

    Reverse hydrolysis by cardosin A: specificity considerations

  • Author/Authors

    A. Cristina Sarmento، نويسنده , , A. and Oliveira، نويسنده , , Clلudia and Pires، نويسنده , , Euclides and Amado، نويسنده , , Francisco W.A. Barros، نويسنده , , Marlene، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2004
  • Pages
    5
  • From page
    33
  • To page
    37
  • Abstract
    Cardosin A, a plant aspartic proteinase, capable of synthesising peptides, was investigated through synthesis of five methyl esters amino acid substrates as amino donors and nine benzyloxycarbonyl amino acid and peptide carboxyl donors. It was found that cardosin A is able to catalyse the synthesis of several peptide bonds, being the preference order for the carboxyl components the following: CBz.Phe>CBz.Trp. Unpredictably, Tyr could not be accepted in P1. Results were compared and discussed according to the known specificity of pepsin, the most studied aspartic proteinase.
  • Keywords
    Cardosin A , aspartic proteinase , Two-phase systems , peptide synthesis , Enzymatic peptide synthesis
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Serial Year
    2004
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Record number

    1716303