Reverse hydrolysis by cardosin A: specificity considerations

A. Cristina Sarmento, Cláudia Oliveira, Euclides Pires, Francisco Amado, Marlene Barros*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)33-37
Number of pages5
JournalJournal of Molecular Catalysis B: Enzymatic
Issue number1
Publication statusPublished - 2 Apr 2004


  • Aspartic proteinase
  • Cardosin A
  • Enzymatic peptide synthesis
  • Peptide synthesis
  • Two-phase systems


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