Activity of Recombinant Dengue 2 Virus NS3 Protease in the Presence of a Truncated NS2B Co-factor, Small Peptide Substrates, and Inhibitors*

@article{Leung2001ActivityOR,
  title={Activity of Recombinant Dengue 2 Virus NS3 Protease in the Presence of a Truncated NS2B Co-factor, Small Peptide Substrates, and Inhibitors*},
  author={D. Leung and Kate Schroder and H. White and Ning Xia Fang and Martin J. Stoermer and G. Abbenante and J. L. Fern{\'a}ndez Mart{\'i}n and Paul R. Young and David P. Fairlie},
  journal={The Journal of Biological Chemistry},
  year={2001},
  volume={276},
  pages={45762 - 45771}
}
Recombinant forms of the dengue 2 virus NS3 protease linked to a 40-residue co-factor, corresponding to part of NS2B, have been expressed in Escherichia coli and shown to be active against para-nitroanilide substrates comprising the P6-P1 residues of four substrate cleavage sequences. The enzyme is inactive alone or after the addition of a putative 13-residue co-factor peptide but is active when fused to the 40-residue co-factor, by either a cleavable or a noncleavable glycine linker. The NS4B… 

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