Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action.

@article{Bansal2012HyperthermophilicAM,
  title={Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action.},
  author={Saurabh Bansal and Ankit Srivastava and Goutam Mukherjee and Ramendra Pati Pandey and Anita Kamra Verma and Prashant Mishra and Bishwajit Kundu},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={2012},
  volume={26 3},
  pages={1161-71}
}
Thermophilic l-asparaginases display high stability and activity at elevated temperatures. However, they are of limited use in leukemia therapy because of their low substrate affinity and reduced activity under physiological conditions. In an attempt to combine stability with activity at physiological conditions, 3 active-site mutants of Pyrococcus furiosus… CONTINUE READING