Beta-aspartylpeptides as substrates of L-asparaginases from Escherichia coli and Erwinia chrysanthemi.
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.
Kelo
Eira
E
Department of Clinical Chemistry, Kuopio University Hospital, Finland. eira.kelo@kuh.fi
Noronkoski
Tiina
T
Stoineva
Ivanka B
IB
Petkov
Dimiter D
DD
Mononen
Ilkka
I
D000970:Antineoplastic Agents / Q000633:toxicity; D001215:Asparaginase / Q000378:metabolism* / Q000633:toxicity; D016974:Dickeya chrysanthemi / Q000201:enzymology*; D004926:Escherichia coli / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism; D054198:Precursor Cell Lymphoblastic Leukemia-Lymphoma / Q000188:drug therapy / Q000378:metabolism; D013379:Substrate Specificity
D000970:Antineoplastic Agents; D009842:Oligopeptides; D001215:Asparaginase