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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Kinetics, inhibition and oligomerization of Epstein-Barr virus protease.

Epstein-Barr virus (EBV) is an omnipresent human virus causing infectious mononucleosis and EBV associated cancers. Its protease is a possible target for antiviral therapy. We studied its dimerization and enzyme kinetics with two enzyme assays based either on the release of paranitroaniline or 7-amino-4-methylcoumarin from labeled pentapeptide (Ac-KLVQA) substrates. The protease is in a monomer-dimer equilibrium where only dimers are active. In absence of citrate the K(d) is 20muM and drops to 0.2muM in presence of 0.5M citrate. Citrate increases additionally the activity of the catalytic sites. The inhibitory constants of different substrate derived peptides and alpha-keto-amide based inhibitors, which have at best a K(i) of 4muM, have also been evaluated.[1]

References

  1. Kinetics, inhibition and oligomerization of Epstein-Barr virus protease. Buisson, M., Rivail, L., Hernandez, J.F., Jamin, M., Martinez, J., Ruigrok, R.W., Burmeister, W.P. FEBS Lett. (2006) [Pubmed]
 
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