EC Number   |
General Information |
Reference |
|---|
   3.4.22.46 | evolution |
significant conformational adaptation by the enzyme is important for substrate recognition, specificity differences between 3Cpro from different picornaviruses, overview |
709535 |
| 3.4.22.46 | malfunction |
the inhibition of LepB results in repressing the cleavage of the signal peptide from the preproteins which would lead to arresting the folding of proteins which are essential for the growth and pathogenesis of Mycobacterium tuberculosis into their active mature conformation |
-, 731252 |
| 3.4.22.46 | metabolism |
functions in the last step of nisin maturation as the leader-peptide peptidase |
731065 |
| 3.4.22.46 | more |
the region encoding leader proteases plays a role in the superinfection exclusion (SIE), a phenomenon in which a primary virus infection prevents a secondary infection with the same or closely related virus |
755647 |
| 3.4.22.46 | physiological function |
foot and mouth disease virus expresses its genetic information as a single polyprotein that is translated from the single-stranded RNA genome. The leader protease, Lbpro, performs the initial cleavage by freeing itself from the growing polypeptide chain. Subsequently, Lbpro cleaves the two homologues of the host cell protein eukaryotic initiation factor 4G, eIF4G. Lbpro possesses specific binding sites at the non-prime side from S1 down to S7 |
717297 |
| 3.4.22.46 | physiological function |
host-dependent separation of the enzyme from the remainder of the polyprotein is essential for suppressing RNA silencing defenses and for efficient viral infection |
732976 |
| 3.4.22.46 | physiological function |
LGP2 cleavage by the Leader protease of aphthoviruses may represent an antagonistic mechanism for immune evasion |
755214 |
| 3.4.22.46 | physiological function |
the enzyme inhibits the host innate immune response by the revention of the synthesis of cytokines such as interferons immediately after infection (brought about by specific proteolytic cleavage of the eukaryotic initiation factor 4G) as well as nuclear factor-kappaB cleavage and the deubiquitination of immune signalling molecules |
731405 |
| 3.4.22.46 | physiological function |
the leader proteinase, Lpro, acts as an interferon-beta antagonist and inhibits IFN-alpha1/beta promoter activation, poly(I:C)-induced IFN-alpha1/beta mRNA expression, and dsRNA-induced type I interferon transcription by decreasing interferon regulatory factor 3/7 in protein levels. Lpro significantly reduced the transcription of multiple IRF-responsive genes |
717188 |
| 3.4.22.46 | physiological function |
the viral RNA genome is translated in the cytoplasm of infected cells as a long polyprotein precursor that is cleaved by virally encoded proteases to release functional proteins needed for the synthesis of new virions. In 10 of 13 cases, 3Cpro performs the cleavages by targeting specific sequences within the polyprotein |
709535 |
