3.4.22.B50: papain-like proteinase 2
This is an abbreviated version, for detailed information about papain-like proteinase 2, go to the full flat file.
responsible for the cleavages located at the N-terminus of the replicase polyprotein
Erv-C, ervatamin-C, mouse hepatitis virus papain-like proteinase 2, papain-like accessory proteases, papain-like cysteine proteinase, papain-like protease, papain-like protease domain 2, papain-like proteinase, PL2-PRO, PL2pro, PLP-2, PLP2, PLpro, SARS-coronavirus papain-like protease, SARS-CoV papain-like protease, SARS-CoV PLpro, severe acute respiratory syndrome coronavirus papain-like protease
General Information on EC 3.4.22.B50 - papain-like proteinase 2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
mutations of residues in the enzyme-ubiquitin interface lead to reduced catalytic activity
arteriviruses lacking PLP2 deubiquitinase activity elicit an enhanced host innate immune response
papain-like protease domain 2 (PLP2) deubiquitinates TANK-binding kinase-1 (TBK1) and reduces its kinase activity, hence inhibits interferon-beta reporter activity and prevents interferon regulatory factor 3 (IRF3) nuclear translocation. The presence of PLP2 stabilizes the hypo-phosphorylated IRF3-TBK1 complex in a dose-dependent manner in the cytoplasm
PLP2 is responsible for the inhibition of both RIG-I and TLR3-dependent induction of interferon alpha/beta expression
the enzyme is one of two cysteine proteases involved in the proteolytic processing of the polyproteins of Severe acute respiratory syndrome coronavirus. It also shows significant in vitro deubiquitinating and de-ISGylating activities
the primary function of the enzyme is to process the viral polyprotein in a coordinated manner. An additional function of the enzyme is stripping ubiquitin and ISG15 from host-cell proteins to aid the coronavirus in the evasion of the host innate immune responses, enzyme innate immune functions, overview
the enzyme strongly inhibits RIG-Iand STING-activated interferon expression. Papain-like protease 2 acts as a viral deubiquitinase to interfere with the RIG-I- and STING-mediated signalling pathway
the enzyme is essential for arterivirus replication by cleaving a site within the viral replicase polyproteins and also removes ubiquitin from cellular proteins. This deubiquitinase activity is a critical factor in arteriviral innate immune evasion
the enzyme comprises the viral polyprotein residues 1541-1858
enzyme structure and function, active site structure with catalytic triad residues, Cys112, His273 and Asp287 and the oxyanion hole-stabilizing residue Trp107, and catalytic mechanism, detailed overview. The fingers domain of PLpro, which contains a zinc ion that is tetrahedrally coordinated by four cysteines, is essential for catalysis because it maintains the structural integrity of the enzyme