Background: Helicobacter pylori L-asparaginase is a recently isolated bacterial factor able to inhibit the cell-cycle of exposed cells, but also a potential platform to develop new anti-cancer drugs, due to its remarkable selectivity for L-asparagine. Methods: To generate new, useful variants of the enzyme, site directed mutagenesis and random mutagenesis are being used to introduce modifications of the protein. The latter method required finding a powerful selection method to isolate interesting mutants. Results: Site-directed mutants generated for L-asparaginase show different levels of activity both towards L-asparagine and L-glutamine. Selecetion of random mutants is still ongoing. Conclusions: Dissection of L- asparaginase activity towards different substrates can be useful to generate better anti-cancer therapeutics.
Generation of Mutants of Helicobacter pylori L-Asparaginase
COVINI, DANIELE;PASQUETTO, MARIA VALENTINA;VECCHIA, LUCA;Maggi M.;VALENTINI, GIOVANNA;CHIARELLI, LAURENT;SCOTTI, CLAUDIA
2012-01-01
Abstract
Background: Helicobacter pylori L-asparaginase is a recently isolated bacterial factor able to inhibit the cell-cycle of exposed cells, but also a potential platform to develop new anti-cancer drugs, due to its remarkable selectivity for L-asparagine. Methods: To generate new, useful variants of the enzyme, site directed mutagenesis and random mutagenesis are being used to introduce modifications of the protein. The latter method required finding a powerful selection method to isolate interesting mutants. Results: Site-directed mutants generated for L-asparaginase show different levels of activity both towards L-asparagine and L-glutamine. Selecetion of random mutants is still ongoing. Conclusions: Dissection of L- asparaginase activity towards different substrates can be useful to generate better anti-cancer therapeutics.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
