Author: Xufang Deng; Yafang Chen; Anna M. Mielech; Matthew Hackbart; Kristina R. Kesely; Robert C. Mettelman; Amornrat O’Brien; Mackenzie E. Chapman; Andrew D. Mesecar; Susan C. Baker
Title: Structure-Guided Mutagenesis Alters Deubiquitinating Activity and Attenuates Pathogenesis of a Murine Coronavirus Document date: 2019_9_25
ID: l3qp0n9f_1
Snippet: Since one of the primary goals of this study is to understand the contribution of DUB 118 activity to viral replication and pathogenesis, we next focused on quantitating further the effects 119 of the D1772A mutant on the steady-state kinetic parameters of MHV PLP2 toward the three 120 different substrates (Fig. 2B) . The RLRGG-AMC peptide substrate is often used as surrogate of 121 the viral polyprotein substrate and the kinetic data in Fig. 2B .....
Document: Since one of the primary goals of this study is to understand the contribution of DUB 118 activity to viral replication and pathogenesis, we next focused on quantitating further the effects 119 of the D1772A mutant on the steady-state kinetic parameters of MHV PLP2 toward the three 120 different substrates (Fig. 2B) . The RLRGG-AMC peptide substrate is often used as surrogate of 121 the viral polyprotein substrate and the kinetic data in Fig. 2B show that this substrate is still well-122 recognized and cleaved by the D1772A mutant. In fact, we observed a small rate enhancement in 123 the catalytic efficiency (i.e., kcat/Km) compared to the wild-type enzyme.
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