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Information on EC 3.4.22.B14 - papain-like proteinase 1 and Organism(s) Murine coronavirus and UniProt Accession P0C6V1

for references in articles please use BRENDA:EC3.4.22.B14
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.B14 papain-like proteinase 1
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This record set is specific for:
Murine coronavirus
UNIPROT: P0C6V1
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Word Map
The taxonomic range for the selected organisms is: Murine coronavirus
The enzyme appears in selected 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, plp1 proteinase, papain-like proteinase 1, first papain-like cysteine proteinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C16.001
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mouse hepatitis virus papain-like proteinase 1
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PL1-PRO
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PLP-1
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PLP1
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ORF 1a polyprotein + H2O
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ORF 1a polyprotein + H2O
?
show the reaction diagram
additional information
?
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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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
reaction is significantly more efficient at 22°C than when carried out at 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
Murine coronavirus (P0C6V1), Murine coronavirus, Murine coronavirus JHM (P0C6V1)
Manually annotated by BRENDA team
Teng, H.; Weiss, S.R.
Further in vitro characterization of mouse hepatitis virus papain-like proteinase 1: cleavage sequence requirements within pp1a
J. Neurovirol.
8
143-149
2002
Murine coronavirus (P0C6V1), Murine coronavirus JHM (P0C6V1)
Manually annotated by BRENDA team
Bonilla, P.J.; Hughes, S.A.; Pinon, J.D.; Weiss, S.R.
Characterization of the leader papain-like proteinase of MHV-A59: identification of a new in vitro cleavage site
Virology
209
489-497
1995
Murine coronavirus (P0C6V1), Murine coronavirus JHM (P0C6V1)
Manually annotated by BRENDA team