Product release is rate-limiting for catalytic processing by the Dengue virus protease.

ABSTRACT: Dengue Virus (DENV) is the most prevalent global arbovirus, yet despite an increasing burden to health care there are currently no therapeutics available to treat infection. A potential target for antiviral drugs is the two-component viral protease NS2B-NS3pro, which is essential for viral replication. Interactions between the two components have been investigated here by probing the effect on the rate of enzyme catalysis of key mutations in a mobile loop within NS2B that is located at the interface of the two components. Steady-state kinetic assays indicated that the mutations greatly affect catalytic turnover. However, single turnover and fluorescence experiments have revealed that the mutations predominantly affect product release rather than substrate binding. Fluorescence analysis als

SUBMITTER: Shannon AE 

PROVIDER: S-EPMC5126634 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature