EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
3.4.22.B50 | MHV substrate |
- |
Alphacoronavirus |
? |
- |
? |
3.4.22.B50 | more |
Cys1715 is a catalytic residue of PLP2 |
Murine coronavirus |
? |
- |
? |
3.4.22.B50 | more |
no in vitro cleavage of the ORF 1a polyprotein in cis or in trans can be detected with PLP-2 expressed either as a polypeptide, including flanking viral sequences, or as an MBP fusion protein |
Murine coronavirus |
? |
- |
? |
3.4.22.B50 | more |
the enzyme is one of three distinct viral proteases (PLP1, PLP2 and 3CLpro) involved in processing of the replicase polyprotein |
Murine coronavirus |
? |
- |
? |
3.4.22.B50 | more |
SARS-CoV PLP2 does not cleave HCoV.229E and IBV substrates |
Alphacoronavirus |
? |
- |
? |
3.4.22.B50 | more |
proteolytic processing of the human coronavirus 229E. PL2pro is able to cleave the nsp1-nsp2 cleavage site. PL2pro plays a universal and essential proteolytic role that appears to be assisted by the PL1pro paralog at specific sites |
Human coronavirus 229E |
? |
- |
? |
3.4.22.B50 | more |
the core domain of PLP2 has in vivo deubiquitinase and DeISGylation activity |
Human coronavirus NL63 |
? |
- |
? |
3.4.22.B50 | more |
the enzyme cannot cleave Z-KAGG-7-amido-4-methylcoumarin |
infectious bronchitis virus |
? |
- |
? |
3.4.22.B50 | more |
SARS-CoV PLP2 does not cleave HCoV.229E and IBV substrates |
Alphacoronavirus SARS-CoV |
? |
- |
? |
3.4.22.B50 | replicase polyprotein + H2O |
PLP2 cleaves a substrate encoding the first predicted membrane-spanning domain, MP1, of the replicase polyprotein. Processing the replicase polyprotein at this site generates the p150 replicase intermediate that is likely critical for embedding the replicase complex into cellular membranes. The enzyme acts efficiently in trans |
Murine coronavirus |
? |
- |
? |