Selected article for: "enzyme substrate and extended conformation"
Author: Fung, To Sing; Liu, Ding Xiang
Title: Post-translational modifications of coronavirus proteins: roles and function
  • Document date: 2018_5_21
    • ID: 38c28tw1_45
    Snippet: In terms of biochemistry, PLPro from different coronaviruses seems to have slightly different substrate specificities and enzyme properties. SARS-CoV PLPro greatly prefers K48-linked to K63-linked ubiquitin chains. The specificity of SARS-CoV PLPro toward polyUb(K48) was proposed to be determined by its extended conformation and binding via two contact sites [186] . In contrast, the PLPro of MERS-CoV cleaves polyUb chains with broad linkage speci.....
    Document: In terms of biochemistry, PLPro from different coronaviruses seems to have slightly different substrate specificities and enzyme properties. SARS-CoV PLPro greatly prefers K48-linked to K63-linked ubiquitin chains. The specificity of SARS-CoV PLPro toward polyUb(K48) was proposed to be determined by its extended conformation and binding via two contact sites [186] . In contrast, the PLPro of MERS-CoV cleaves polyUb chains with broad linkage specificity. Also, whereas MERS-CoV PLPro cleaves polyUb chains one Ub at a time, SARS-CoV PLPro cleaves K48-linked polyUb chain in a 'di-distributive' manner -that is, removing a di-Ub moiety at a time [187] .

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