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
Link To Document :
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