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- W2069634512 abstract "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 20 μM and drops to 0.2 μM in presence of 0.5 M citrate. Citrate increases additionally the activity of the catalytic sites. The inhibitory constants of different substrate derived peptides and α‐keto‐amide based inhibitors, which have at best a K i of 4 μM, have also been evaluated." @default.
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- W2069634512 date "2006-11-14" @default.
- W2069634512 modified "2023-10-17" @default.
- W2069634512 title "Kinetics, inhibition and oligomerization of Epstein-Barr virus protease" @default.
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- W2069634512 doi "https://doi.org/10.1016/j.febslet.2006.11.006" @default.
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