Selected article for: "catalytic triad and serine protease"
Author: Sun, Di; Chen, Shun; Cheng, Anchun; Wang, Mingshu
Title: Roles of the Picornaviral 3C Proteinase in the Viral Life Cycle and Host Cells
  • Document date: 2016_3_17
    • ID: 07nfb69o_9
    Snippet: Picornavirus 3C pro s possesses a conserved Cys-His-Asp/Glu catalytic triad within the active site. This structure is similar to the Ser-His-Asp catalytic triad of serine proteases, except that third residue of the triad plays a less important catalytic role than in a serine protease. The catalytic residues in HAV include Cys-172 as a nucleophile and His-44 as a general base to form a Cys-His dyad [18] . Proteolytic mechanism studies in EV71 have.....
    Document: Picornavirus 3C pro s possesses a conserved Cys-His-Asp/Glu catalytic triad within the active site. This structure is similar to the Ser-His-Asp catalytic triad of serine proteases, except that third residue of the triad plays a less important catalytic role than in a serine protease. The catalytic residues in HAV include Cys-172 as a nucleophile and His-44 as a general base to form a Cys-His dyad [18] . Proteolytic mechanism studies in EV71 have shown that an uncharacterized residue Arg39 is involved in the proteolysis reaction by altering the distance to Glu71 as a charge neutralizer. Arg39 residue is conserved among CVB3, simian enterovirus (SEV) and FMDV 3C pro whereas a conserved substitution of R39K is present in the 3C pro of porcine enterovirus (PEV). In addition, Arg39 is replaced by an uncharged threonine or serine in the 3C pro of PV, HRV and HAV, thereby indicating that Arg39 cannot be a neutralizer [19] . His40, a catalytic residue of triad, adopts two conformations as follows: a productive conformation that has been observed in most picornaviral 3C pro s and accounts for 39%; and a nonproductive conformation in which an imidazole side chain is positioned outside the hydrogen bonding distance to Cys-147, accounting for 61%. Thus, the negatively charged carboxylate side chain of Glu71 plays a critical role in maintaining the entire architecture of the active site and in stabilizing the productive conformation of His40 [19] .

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