EC Number |
General Information |
Reference |
---|
3.4.22.B50 | physiological function |
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 |
718275 |
3.4.22.B50 | physiological function |
PLP2 is responsible for the inhibition of both RIG-I and TLR3-dependent induction of interferon alpha/beta expression |
718347 |
3.4.22.B50 | malfunction |
mutations of residues in the enzyme-ubiquitin interface lead to reduced catalytic activity |
731069 |
3.4.22.B50 | more |
the enzyme comprises the viral polyprotein residues 1541-1858 |
731069 |
3.4.22.B50 | physiological function |
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 |
731069 |
3.4.22.B50 | more |
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 |
731149 |
3.4.22.B50 | physiological function |
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 |
731149 |
3.4.22.B50 | physiological function |
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 |
732257 |
3.4.22.B50 | malfunction |
arteriviruses lacking PLP2 deubiquitinase activity elicit an enhanced host innate immune response |
732827 |
3.4.22.B50 | physiological function |
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 |
732827 |