Abstract
Human rhinovirus (HRV) 3C protease was inactivated by a series of S-nitrosothiols. These compounds exhibited different inhibitory activities in a time- and concentration-dependent manner with second-order rate constants (k(inact)/K(I)) ranging from 131 to 5360 M-1 min-1. The inactive enzyme could be re-activated by DTT, GSH and ascorbate, which indicated the inactivation mechanism was through an S-transnitrosylation process. (C) 2000 Elsevier Science Ltd.
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CITATION STYLE
Xian, M., Wang, Q. M., Chen, X., Wang, K., & Wang, P. G. (2000). S-nitrosothiols as novel, reversible inhibitors of human rhinovirus 3C protease. Bioorganic and Medicinal Chemistry Letters, 10(18), 2097–2100. https://doi.org/10.1016/S0960-894X(00)00420-0
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