Journal
FEBS LETTERS
Volume 528, Issue 1-3, Pages 130-132Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)03273-8
Keywords
enzyme kinetics; leukemia; substrate specificity
Ask authors/readers for more resources
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-aspartylanineamide, 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 -aspartylpeptides and suggest that L-asparaginase therapy may affect the metabolism of P-aspartylpeptides present in human body. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available