β-aspartylpeptides as substrates of L-asparaginases from Escherichia coli and Erwinia chrysanthemi
β-aspartylpeptides as substrates of L-asparaginases from Escherichia coli and Erwinia chrysanthemi
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DOI：
10.1016/s0014-5793(02)03273-8
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发表时间：
2002-09-25
期刊：
影响因子：
3.5
通讯作者：
Mononen, I
中科院分区：
文献类型：
--
作者：
Kelo, E;Noronkoski, T;Mononen, I
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.
