Reverse hydrolysis by cardosin A: specificity considerations

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

doi:10.1016/j.molcatb.2004.02.001

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 journal › Article › peer-review

12 Citations (Scopus)

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.

Original language	English
Pages (from-to)	33-37
Number of pages	5
Journal	Journal of Molecular Catalysis B: Enzymatic
Volume	28
Issue number	1
DOIs	https://doi.org/10.1016/j.molcatb.2004.02.001
Publication status	Published - 2 Apr 2004

Keywords

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

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10.1016/j.molcatb.2004.02.001

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title = "Reverse hydrolysis by cardosin A: specificity considerations",

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 = "Aspartic proteinase, Cardosin A, Enzymatic peptide synthesis, Peptide synthesis, Two-phase systems",

author = "Sarmento, \{A. Cristina\} and Cl{\'a}udia Oliveira and Euclides Pires and Francisco Amado and Marlene Barros",

year = "2004",

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doi = "10.1016/j.molcatb.2004.02.001",

language = "English",

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pages = "33--37",

journal = "Journal of Molecular Catalysis B: Enzymatic",

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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 - https://www.scopus.com/pages/publications/1842535399

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 -

Reverse hydrolysis by cardosin A: specificity considerations

Abstract

Keywords

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