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.
Word Map on EC 3.4.22.B50
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3.4.22.B50
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polyproteins
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replicase
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coronaviruses
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3clpro
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isg15
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3c-like
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mhv-a59
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nsp3
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coronaviral
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pp1ab
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medicine
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drug development
- 3.4.22.B50
- polyproteins
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replicase
- coronaviruses
- 3clpro
- isg15
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3c-like
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mhv-a59
- nsp3
- coronaviral
- pp1ab
- medicine
- drug development
Reaction
responsible for the cleavages located at the N-terminus of the replicase polyprotein =
Synonyms
Erv-C, ervatamin-C, mouse hepatitis virus papain-like proteinase 2, papain-like accessory protease, 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
ECTree
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Substrates Products
Substrates Products on EC 3.4.22.B50 - papain-like proteinase 2
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REACTION DIAGRAM
Dabcyl-FRLKGGAPIKGV-Edans + H2O
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SARS-CoV-derived substrate
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?
FRLKGG-4-nitroanilide + H2O
FRLKGG + 4-nitroaniline
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?
N-benzoyl-Phe-Val-Arg-4-nitroanilide + H2O
N-benzoyl-Phe-Val-Arg + 4-nitroaniline
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?
polyubiquitin + H2O
monoubiquitin + ?
the enzyme cleaves Lys48- and Lys63-linked polyubiquitin to monoubiquitin but not linear polyubiquitin
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?
RELNGGAVTRYV + H2O
AVTYRV + RELNGG
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12 mer oligopeptide containing Gly180-Ala181, 5% cleavage
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replicase polyprotein + H2O
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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
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?
RLRGG-7-amido-4-methylcoumarin + H2O
RLRGG + 7-amino-4-methylcoumarin
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?
ubiquitin-7-amido-4-trifluoro-methyl-coumarin + H2O
ubiquitin + 7-amino-4-trifluoro-methyl-coumarin
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?
ubiquitin-7-amido-4-trifluoromethylcoumarin + H2O
ubiquitin + 7-amino-4-trifluoromethylcoumarin
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
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?
ubiquitinated RIG-I + H2O
deubiquitinated RIG-I + ubiquitin
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ubiquitinated STING + H2O
deubiquitinated STING + ubiquitin
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viral replicase polyprotein + H2O
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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.
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?
Z-KKAG-7-amido-4-methylcoumarin + H2O
Z-KKAG + 7-amino-4-methylcoumarin
the catalytic efficiency toward Z-KKAG-7-amido-4-methylcoumarin is 5times higher than that for Z-LRGG-7-amido-4-methylcoumarin
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?
Z-LRGG-7-amido-4-methylcoumarin + H2O
Z-LRGG + 7-amino-4-methylcoumarin
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?
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fluorogenic substrate
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Abz-FRLKGGAPIKGV-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
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fluorogenic substrate
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?
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12 mer oligopeptide containing Gly818-Ala819, 100% cleavage
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FRLKGGAPIKGV
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12 mer oligopeptide containing Gly818-Ala819, 100% cleavage
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?
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12 mer oligopeptide containing Gly2740-Lys2741, 29% cleavage
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ISLKGGKIVSTC
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12 mer oligopeptide containing Gly2740-Lys2741, 29% cleavage
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ubiquitin + H2O
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the enzyme cleaves the LRGG tail of ubiquitin
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ubiquitin + H2O
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the enzyme processes both K-48 and K-63 linked polyubiquitin chains
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SARS-CoV PLP2 does not cleave HCoV.229E and IBV substrates
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additional information
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SARS-CoV PLP2 does not cleave HCoV.229E and IBV substrates
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additional information
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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
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additional information
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the core domain of PLP2 has in vivo deubiquitinase and DeISGylation activity
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additional information
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the enzyme cannot cleave Z-KAGG-7-amido-4-methylcoumarin
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additional information
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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
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additional information
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the enzyme is one of three distinct viral proteases (PLP1, PLP2 and 3CLpro) involved in processing of the replicase polyprotein
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?