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_3
Snippet: The Ub-AMC substrate, on the other hand, is poorly recognized and cleaved by the 125 D1772A mutant compared to the wild-type enzyme. The wild-type enzyme normally interacts 126 strongly with Ub-AMC with a Km value of 0.67 µM. However, mutation of D1772 to an alanine 127 significantly disrupts the interaction with ubiquitin, making it impossible to saturate MHV PLP2 128 All rights reserved. No reuse allowed without permission......
Document: The Ub-AMC substrate, on the other hand, is poorly recognized and cleaved by the 125 D1772A mutant compared to the wild-type enzyme. The wild-type enzyme normally interacts 126 strongly with Ub-AMC with a Km value of 0.67 µM. However, mutation of D1772 to an alanine 127 significantly disrupts the interaction with ubiquitin, making it impossible to saturate MHV PLP2 128 All rights reserved. No reuse allowed without permission.
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