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Information on EC 3.4.22.B14 - papain-like proteinase 1
for references in articles please use BRENDA:EC3.4.22.B14preliminary BRENDA-supplied EC number
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EC Tree
3.4.22.B14 papain-like proteinase 1Specify your search results
Word Map
- 3.4.22.B14
- polyproteins
- pp1a
- sars-cov-2
-
rna-dependent
- coronaviruses
-
mhv-a59
-
preproinsulin
- nsp3
- 3clpro
- plpros
- remdesivir
- coronaviral
- ace2
-
3-chymotrypsin-like
-
positive-strand
-
autoproteolytic
-
admet
-
wistar-furth
The enzyme appears in viruses and cellular organisms
Reaction Schemes
papain-like proteinase 1 is responsible for cleavages located at the N-terminus of the replicase polyprotein
Synonyms
plp-1, pl1pro, replicase polyprotein 1a, first papain-like cysteine proteinase, plp1 proteinase, papain-like proteinase 1, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C16.001
-
-
-
-
mouse hepatitis virus papain-like proteinase 1
-
-
-
-
PL1-PRO
-
-
-
-
PL1pro
PLP-1
-
-
-
-
PLP1
PLpro
replicase polyprotein 1a
PLP1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
papain-like proteinase 1 is responsible for cleavages located at the N-terminus of the replicase polyprotein
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-[[4-(dimethylamino)phenyl]azo]benzoic acid-MYNKMGGGDKTVSF-(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid) amide + H2O
?
L-Arg-L-Leu-L-Arg-Gly-Gly-7-amido-4-methylcoumarin + H2O
L-Arg-L-Leu-L-Arg-Gly-Gly + 7-amino-4-methylcoumarin
-
-
-
-
?
proISG + H2O
?
i.e. proenzyme of interferon-stimulated gene product 15
-
-
?
tetra-ubiquitin + H2O
2 di-ubiquitin
-
-
-
-
?
ubiquitinated RIG-I + H2O
ubiquitin + RIG-I
-
substrate is a key fegulator in the IFN signaling pathway
-
-
?
ubiquitinated STING + H2O
ubiquitin + STINGI
-
substrate is a key fegulator in the IFN signaling pathway
-
-
?
4-[[4-(dimethylamino)phenyl]azo]benzoic acid-MYNKMGGGDKTVSF-(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid) amide + H2O
?
-
-
-
?
4-[[4-(dimethylamino)phenyl]azo]benzoic acid-MYNKMGGGDKTVSF-(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid) amide + H2O
?
-
-
-
?
ISG15-7-amido-4-methylcoumarin + H2O
ISG15 + 7-amino-4-methylcoumarin
-
-
-
-
?
ISG15-7-amido-4-methylcoumarin + H2O
ISG15 + 7-amino-4-methylcoumarin
-
-
-
-
?
KAGG-7-amido-4-methylcoumarin + H2O
KAGG + 7-amino-4-methylcoumarin
-
-
-
?
KAGG-7-amido-4-methylcoumarin + H2O
KAGG + 7-amino-4-methylcoumarin
-
-
-
?
KKAG-7-amido-4-methylcoumarin + H2O
KKAG + 7-amino-4-methylcoumarin
-
-
-
?
KKAG-7-amido-4-methylcoumarin + H2O
KKAG + 7-amino-4-methylcoumarin
-
-
-
?
LRGG-7-amido-4-methylcoumarin + H2O
LRGG + 7-amino-4-methylcoumarin
-
-
-
?
LRGG-7-amido-4-methylcoumarin + H2O
LRGG + 7-amino-4-methylcoumarin
-
-
-
?
ORF 1a polyprotein + H2O
?
cleavage sites are: Gly247-/-Val248 and Gly821-/-Val822. PLP-1 is responsible for the cleavage of the amino-terminal protein p28
-
-
?
ORF 1a polyprotein + H2O
?
cleavage in cis and in trans. PLP-1 cleavage activity appears to be optimal when both enzyme and substrate are present as part of polyproteins, as they are in the virus replication cycle
-
-
?
ORF 1a polyprotein + H2O
?
the enzyme is involved in processing of ORF 1a polyprotein into mature replicase-related polypeptides
-
-
?
ORF 1a polyprotein + H2O
?
cleavage in cis and in trans. PLP-1 cleavage activity appears to be optimal when both enzyme and substrate are present as part of polyproteins, as they are in the virus replication cycle
-
-
?
ORF 1a polyprotein + H2O
?
cleavage sites are: Gly247-/-Val248 and Gly821-/-Val822. PLP-1 is responsible for the cleavage of the amino-terminal protein p28
-
-
?
ORF 1a polyprotein + H2O
?
the enzyme is involved in processing of ORF 1a polyprotein into mature replicase-related polypeptides
-
-
?
ORF 1a polyprotein + H2O
nsp1 + nsp2 + nsp3
-
SARS coronavirus replicase polyproteins pp1a and pp1ab are predicted to be processed into 16 nonstructural proteins, NSP2-3 intermediate identified
identified products
-
?
ORF 1a polyprotein + H2O
nsp1 + nsp2 + nsp3
-
SARS coronavirus replicase polyproteins pp1a and pp1ab are predicted to be processed into 16 nonstructural proteins, NSP2-3 intermediate identified
identified products
-
?
ubiquitin-7-amido-4-methylcoumarin + H2O
ubiquitin + 7-amino-4-methylcoumarin
-
-
-
-
?
ubiquitin-7-amido-4-methylcoumarin + H2O
ubiquitin + 7-amino-4-methylcoumarin
-
-
-
-
?
ubiquitin-7-amido-4-methylcoumarin + H2O
ubiquitin + 7-amino-4-methylcoumarin
-
-
-
?
ubiquitin-7-amido-4-methylcoumarin + H2O
ubiquitin + 7-amino-4-methylcoumarin
-
-
-
?
additional information
?
-
PLpro can degrade Lys48- and Lys63-linked polyubiquitin chains to monoubiquitin but not linear polyubiquitin
-
-
?
additional information
?
-
PLpro can degrade Lys48- and Lys63-linked polyubiquitin chains to monoubiquitin but not linear polyubiquitin
-
-
?
additional information
?
-
-
enzyme is able to cleave ubiquitin mutant L73P in K6-, K11-, K48- and K63-linked di-ubiquitin chains. Cleavage rates with MERS PLpro are nearly identical against ubiquitin chains of various lengths
-
-
?
additional information
?
-
-
MERS PLpro has an absolute requirement for Gly in the P2 position, but can accommodate a wide variety of hydrophobic amino acids in both the P3 and P4 positions. The most preferred amino acid in P3 is Leu, followed by Arg, Lys and hydrophobic residues. The most preferred amino acid in P4 is also Leu, followed by mostly hydrophobic residues
-
-
?
additional information
?
-
viral substrates translated from pSPDELTAMscN1S1, p28, p43 and p70, efficient cleavage requires a substrate greater than 69000 Da
-
-
?
additional information
?
-
-
viral substrates translated from pSPDELTAMscN1S1, p28, p43 and p70, efficient cleavage requires a substrate greater than 69000 Da
-
-
?
additional information
?
-
the virus can regulate in vivo proteinase activity through self inactivation of PLP-1. The lack of p50 production in cells infected with the mouse hepatitis virus strain JHM may regulate PLP-1 activity differently from MHV-59
-
-
?
additional information
?
-
the virus can regulate in vivo proteinase activity through self inactivation of PLP-1. The lack of p50 production in cells infected with the mouse hepatitis virus strain JHM may regulate PLP-1 activity differently from MHV-59
-
-
?
additional information
?
-
viral substrates translated from pSPDELTAMscN1S1, p28, p43 and p70, efficient cleavage requires a substrate greater than 69000 Da
-
-
?
additional information
?
-
-
interactions of PLP1 with CS1 and CS2 are critical for protein processing and suggest that the interactions play specific roles in regulation of the functions of nsp1, 2, and 3 in viral RNA synthesis
-
-
?
additional information
?
-
-
SARS PLpro recognizes a K48-linked tri-Ub as a minimal unit for ubiquitin chain processing
-
-
?
additional information
?
-
PL1pro cleaves a peptide mimicking the cognate nsp2-nsp3 cleavage site, has deubiquitinating activity in an in vitro cleavage assay and displays a slight preference for Lys48-linked polyubiquitin chains over Lys63-linked ones
-
-
?
additional information
?
-
PL1pro cleaves a peptide mimicking the cognate nsp2-nsp3 cleavage site, has deubiquitinating activity in an in vitro cleavage assay and displays a slight preference for Lys48-linked polyubiquitin chains over Lys63-linked ones
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ORF 1a polyprotein + H2O
?
cleavage in cis and in trans. PLP-1 cleavage activity appears to be optimal when both enzyme and substrate are present as part of polyproteins, as they are in the virus replication cycle
-
-
?
ORF 1a polyprotein + H2O
?
the enzyme is involved in processing of ORF 1a polyprotein into mature replicase-related polypeptides
-
-
?
ORF 1a polyprotein + H2O
?
cleavage in cis and in trans. PLP-1 cleavage activity appears to be optimal when both enzyme and substrate are present as part of polyproteins, as they are in the virus replication cycle
-
-
?
ORF 1a polyprotein + H2O
?
the enzyme is involved in processing of ORF 1a polyprotein into mature replicase-related polypeptides
-
-
?
additional information
?
-
the virus can regulate in vivo proteinase activity through self inactivation of PLP-1. The lack of p50 production in cells infected with the mouse hepatitis virus strain JHM may regulate PLP-1 activity differently from MHV-59
-
-
?
additional information
?
-
the virus can regulate in vivo proteinase activity through self inactivation of PLP-1. The lack of p50 production in cells infected with the mouse hepatitis virus strain JHM may regulate PLP-1 activity differently from MHV-59
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,6-dimethyl-N-[(R)-1-(2-naphthyl)ethyl]benzamide
-
-
2,N-dimethyl-N-[(R)-1-(2-naphthyl)ethyl]benzamide
-
-
2-methoxy-N-[(R)-1-(2-naphthyl)ethyl]benzamide
-
-
2-methoxymethyl-5-nitrobenzoic acid methyl ester
-
-
2-methyl-N-[(R)-1-(1-naphthyl)ethyl]benzamide
-
-
2-methyl-N-[1-(naphthalen-2-yl)ethyl]benzamide
-
-
3-methoxy-N-[(R)-1-(2-naphthyl)ethyl]benzamide
-
-
3-methyl-N-[(R)-1-(2-naphthyl)ethyl]benzamide
-
-
4-amino-N-[(R)-1-(1-naphthyl)ethyl]benzamide
-
-
4-amino-N-[(R)-1-(2-naphthyl)ethyl]benzamide
-
-
4-methoxy-N-[(R)-1-(2-naphthyl)ethyl]benzamide
-
-
4-methyl-N-[(R)-1-(2-naphthyl)ethyl]benzamide
-
-
5-amino-2-methoxymethyl-N-[1-methyl-1-(1-naphthyl)ethyl]benzamide
-
-
5-amino-2-methyl-N-[(R)-1-(1-naphthyl)ethyl]benzamide
-
-
5-amino-2-methyl-N-[1-methyl-1-(1-naphthyl)ethyl]benzamide
-
-
5-cyano-2-methyl-N-[1-methyl-1-(1-naphthyl)ethyl]benzamide
-
-
5-iodo-2-methyl-N-[1-methyl-1-(1-naphthyl)ethyl]benzamide
-
-
5-methylamino-2-methyl-N-[(R)-1-(1-naphthyl)ethyl]benzamide
-
-
5-N-acetylamino-2-methyl-N-[(R)-1-(1-naphthyl)ethyl]benzamide
-
-
5-N-tert-butoxycarbonylmethylamino-2-methyl-N'-[(R)-1-(1-naphthyl)ethyl]benzamide
-
-
E-64d
-
membrane-permeable do the irreversible cysteine proteinase inhibitor E-64 blocks cleavage of p65 in vivo
leupeptin
-
blocks the ability of PLP1 to cleave p28 in vitro but not in vivo due to permeability and toxicity issues
N-methyl-5-methylamino-2-methyl-N'-[(R)-1-(1-naphthyl)ethyl]benzamide
-
-
ZnCl2
-
blocks the ability of PLP1 to cleave p28 in vitro but not in vivo due to permeability and toxicity issues
additional information
-
not inhibited by 2-hydroxy-N-[(R)-1-(2-naphthyl)ethyl]benzamide, 4-N'-tert-butoxycarbonylamino-N-[(R)-1-(2-naphthyl)ethyl]-benzamide, 2-methyl-N-[1-(2-naphthyl)propyl]benzamide, and 2-methyl-N-[1-(2-naphthyl)benzyl]benzamide
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hepatitis
Further in vitro characterization of mouse hepatitis virus papain-like proteinase 1: cleavage sequence requirements within pp1a.
Hepatitis
Replication of murine hepatitis virus is regulated by papain-like proteinase 1 processing of nonstructural proteins 1, 2, and 3.
Hepatitis
The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond.
Insulin Resistance
Structural characterization of a homopolysaccharide with hypoglycemic activity from the roots of Pueraria lobata.
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0121
2,6-dimethyl-N-[(R)-1-(2-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.0226
2,N-dimethyl-N-[(R)-1-(2-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.09
2-methoxy-N-[(R)-1-(2-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.0014
2-methoxymethyl-5-nitrobenzoic acid methyl ester
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.0023
2-methyl-N-[(R)-1-(1-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.0087
2-methyl-N-[1-(naphthalen-2-yl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.0135
3-methoxy-N-[(R)-1-(2-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.0148
3-methyl-N-[(R)-1-(2-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.0248
4-amino-N-[(R)-1-(1-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.0461
4-amino-N-[(R)-1-(2-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.149
4-methoxy-N-[(R)-1-(2-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.0291
4-methyl-N-[(R)-1-(2-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.0052
5-amino-2-methoxymethyl-N-[1-methyl-1-(1-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.00056
5-amino-2-methyl-N-[(R)-1-(1-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.00056
5-amino-2-methyl-N-[1-methyl-1-(1-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.0111
5-cyano-2-methyl-N-[1-methyl-1-(1-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.0027
5-iodo-2-methyl-N-[1-methyl-1-(1-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.00046
5-methylamino-2-methyl-N-[(R)-1-(1-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.00264
5-N-acetylamino-2-methyl-N-[(R)-1-(1-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.0048
5-N-tert-butoxycarbonylmethylamino-2-methyl-N'-[(R)-1-(1-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
0.0013
N-methyl-5-methylamino-2-methyl-N'-[(R)-1-(1-naphthyl)ethyl]benzamide
Severe acute respiratory syndrome-related coronavirus
-
in 50 mM HEPES, pH 7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
reaction is significantly more efficient at 22°C than when carried out at 30°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
severe acute respiratory syndrome coronavirus, Urbani strain
-
-
brenda
human, i.e. SARS-CoV
UniProt
brenda
replicase polyprotein; human, i.e. SARS-CoV
UniProt
brenda
severe acute respiratory syndrome coronavirus, strain Tor2
UniProt
brenda
severe acute respiratory syndrome coronavirus, Urbani strain
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
AY310120
insertion of a bat SARS-CoV PLP into the SARS-CoV genome. The resulting virus replicates like SARS-CoV in Vero cells but is suppressed in IFN competent MA-104 (3.7fold), Calu-3 (2.6fold) and human airway epithelial cells (10.3fold). A protease-independent, anti-IFN function exists in SARS-CoV, but not in a SARS-related, bat-borne virus
physiological function
-
MERS PLpro is both a deubiquitinating and a deISGylating enzyme (ISG15 i.e. ubiquitin-like modifier interferon stimulated gene 15). MERS PLpro shows broad linkage specificity for the cleavage of polyUb chains and cleaves polyUb chains one ubiquitin at a time. Comparison with SARS PLpro
physiological function
-
PL1 can suppress the IFN-beta expression and inhibit the nuclear translocation of interferon regulatory factor 3.The ability to antagonize IFN-beta production is dependent on the intact catalytic activity of PL1. PL1 exerts deubiquitinase activity which strongly inhibits the retinoic acid-induced gene I- and stimulator of interferon gene-dependent IFN expression
physiological function
protease PLpro dose- and time-dependently up-regulates TGF-beta1 and vimentin in A-549 cellsThe TGF-beta1 promoter region between -175 to -60, the Egr-1 binding site, is responsible for TGF-beta1 promoter activation induced by PLpro. PLpro triggers nuclear translocation of Egr-1. In a mouse model with a direct pulmonary injection, PLpro stimulates macrophage infiltration into lung, up-regulating Egr-1, TSP-1, TGF-beta1 and vimentin expression in lung tissues
physiological function
-
SARS PLpro prefers to cleave Lys48-linked polyUb chains and needs a di-Ub moiety as a minimal recognition element. Comaprison with MERS PLpro enzyme
physiological function
SARS-CoV and MERS-CoV PLpros are both capable of fully processing proISG15 from human, mouse, camel and bat within 60 minutes. SARS PLpro is also able to fully process proISG15 from sheep and shrew within that same time but it has little to no activity against jackfish proISG15
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). R1A_CVPPU
4017
18
447352
Swiss-Prot
-
R1A_IBVB
3951
18
441126
Swiss-Prot
-
R1AB_CVBEN
Bovine coronavirus (strain 98TXSF-110-ENT)
7094
16
797266
Swiss-Prot
-
R1AB_SARS
7073
14
790248
Swiss-Prot
-
R1AB_IBVB
6629
18
744540
Swiss-Prot
Secretory Pathway (Reliability: 1)
R1AB_PEDV7
6781
18
753158
Swiss-Prot
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.15 A resolution. PLpro has a short blocking loop BL1-like loop. Access to a conserved catalytic triad consisting of Cys101, His264, and Asp275 is regulated by the flexible loop BL2
in complex with interferon-stimulated gene product 15 proteins from different species
hanging drop vapor diffusion method, using 0.1-0.18 M (NH4)2SO4, 0.1 M MES (pH 6.5), and 30% (w/v) PEG 5000, at 19°C
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D196A
-
mutant is unable to degrade ubiquitinated protein
H183A
-
mutant is unable to degrade ubiquitinated protein
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 75 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into plasmids under T7 promoter control and cotransfected into HeLa-MHVR cells infected with recombinant vaccinia virus
-
expressed in Escherichia coli Rosetta (DE3)pLysS cells
expression in Escherichia coli by using a T7 RNA polymerase promoter system or as a maltose-binding protein fusion protein. With both overexpression systems the recombinant PLP-1 exhibits trans cleavage activity. When PLP-1 is expressed as a polypeptide that includes additional viral sequences at the carboxyl terminus of the predicted PLP-1 domain, a fivefold increase in proteolytic activity is observed
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Teng, H.; Pinon, J.D.; Weiss, S.R.
Expression of murine coronavirus recombinant papain-like proteinase: efficient cleavage is dependent on the lengths of both the substrate and the proteinase polypeptide
J. Virol.
73
2658-2666
1999