TY - JOUR
T1 - Reverse hydrolysis by cardosin A
T2 - specificity considerations
AU - Sarmento, A. Cristina
AU - Oliveira, Cláudia
AU - Pires, Euclides
AU - Amado, Francisco
AU - Barros, Marlene
PY - 2004/4/2
Y1 - 2004/4/2
N2 - 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.
AB - 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.
KW - Aspartic proteinase
KW - Cardosin A
KW - Enzymatic peptide synthesis
KW - Peptide synthesis
KW - Two-phase systems
UR - http://www.scopus.com/inward/record.url?scp=1842535399&partnerID=8YFLogxK
U2 - 10.1016/j.molcatb.2004.02.001
DO - 10.1016/j.molcatb.2004.02.001
M3 - Article
AN - SCOPUS:1842535399
SN - 1381-1177
VL - 28
SP - 33
EP - 37
JO - Journal of Molecular Catalysis B: Enzymatic
JF - Journal of Molecular Catalysis B: Enzymatic
IS - 1
ER -