Beta-aspartylpeptides as substrates of L-asparaginases from Escherichia coli and Erwinia chrysanthemi.
FEBS Lett
; 528(1-3): 130-2, 2002 Sep 25.
Article
em En
| MEDLINE
| ID: mdl-12297292
ABSTRACT
L-Asparaginase is known to catalyze the hydrolysis of L-asparagine to L-aspartic and ammonia, but little is known about its action on peptides. When we incubated L-asparaginases purified either from Escherichia coli or Erwinia chrysanthemi - commonly used as chemotherapeutic agents because of their antitumour activity - with eight small beta-aspartylpeptides such as beta-aspartylserineamide, beta-aspartylalanineamide, beta-aspartylglycineamide and beta-aspartylglycine, we found that both L-asparaginases could catalyze the hydrolysis of five of them yielding L-aspartic acid and amino acids or peptides. Our data show that L-asparaginases can hydrolyze beta-aspartylpeptides and suggest that L-asparaginase therapy may affect the metabolism of beta-aspartylpeptides present in human body.
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Base de dados:
MEDLINE
Assunto principal:
Asparaginase
/
Dickeya chrysanthemi
/
Escherichia coli
Idioma:
En
Ano de publicação:
2002
Tipo de documento:
Article