EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   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 |
? |
- |
? |
| 3.4.22.B50 | viral replicase polyprotein + H2O |
PLP2 is responsible for processing both cleavage sites 2 and 3 to release nsp2 and nsp3. The cleavage sites are identified as FTKLAG-/-GKISFS for CS2 and VAKQGA-/-GFKRTY for CS3. |
Human coronavirus NL63 |
? |
- |
? |
| 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 |
SARS-CoV PLP2 does not cleave HCoV.229E and IBV substrates |
Alphacoronavirus |
? |
- |
? |
| 3.4.22.B50 | more |
SARS-CoV PLP2 does not cleave HCoV.229E and IBV substrates |
Alphacoronavirus SARS-CoV |
? |
- |
? |
| 3.4.22.B50 | Dabcyl-FRLKGGAPIKGV-Edans + H2O |
SARS-CoV-derived substrate |
porcine epidemic diarrhea virus |
? |
- |
? |
| 3.4.22.B50 | Z-KKAG-7-amido-4-methylcoumarin + H2O |
the catalytic efficiency toward Z-KKAG-7-amido-4-methylcoumarin is 5times higher than that for Z-LRGG-7-amido-4-methylcoumarin |
infectious bronchitis virus |
Z-KKAG + 7-amino-4-methylcoumarin |
- |
? |
| 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 | ubiquitin-7-amido-4-trifluoromethylcoumarin + H2O |
the enzyme catalyzes proteolytic processing of the viral polyprotein and also shows significant in vitro deubiquitinating and de-ISGylating activities. The enzyme binds ubiquitin, the ubiquitin core makes mostly hydrophilic interactions with the enzyme, while the Leu-Arg-Gly-Gly C-terminus of ubiquitin is located in the catalytic cleft of the enzyme. The ubiquitin core binds to the palm, thumb and fingers domains of the enzyme, while its final four C-terminal residues bind into a narrow channel by a network of hydrogen bonds and reach towards the active site |
Severe acute respiratory syndrome-related coronavirus |
ubiquitin + 7-amino-4-trifluoromethylcoumarin |
- |
? |
