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Information on EC 3.4.22.B50 - papain-like proteinase 2 and Organism(s) Tabernaemontana divaricata and UniProt Accession P83654

for references in articles please use BRENDA:EC3.4.22.B50
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.B50 papain-like proteinase 2
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Tabernaemontana divaricata
UNIPROT: P83654
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Word Map
The taxonomic range for the selected organisms is: Tabernaemontana divaricata
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
responsible for the cleavages located at the N-terminus of the replicase polyprotein
Synonyms
sars-cov plpro, papain-like proteinase, papain-like cysteine proteinase, plp-2, pl2pro, ervatamin-c, erv-c, papain-like protease domain 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
mouse hepatitis virus papain-like proteinase 2
-
-
-
-
PL2-PRO
-
-
-
-
PLP-2
-
-
-
-
PLP2
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
851883-30-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
azocasein + H2O
?
show the reaction diagram
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
?
N-benzoyl-Phe-Val-Arg-4-nitroanilide + H2O
N-benzoyl-Phe-Val-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-cysteine
20 mM used in assay conditions
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09687 - 0.1769
N-benzoyl-Phe-Val-Arg-4-nitroanilide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23 - 2.65
N-benzoyl-Phe-Val-Arg-4-nitroanilide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8 - 14.87
N-benzoyl-Phe-Val-Arg-4-nitroanilide
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0001712 - 0.000349
E-64
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30.78
wild type enzyme, with azocasein as substrate, in 50 mM Na-acetate buffer pH 5.0, at 60°C
63.11
mutant enzyme S32T/A67Y, with azocasein as substrate, in 50 mM Na-acetate buffer pH 5.0, at 60°C
73.63
mutant enzyme S32T, with azocasein as substrate, in 50 mM Na-acetate buffer pH 5.0, at 60°C
86.95
mutant enzyme A67Y, with azocasein as substrate, in 50 mM Na-acetate buffer pH 5.0, at 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8
more than 50% activity between pH 4.5 and 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ERVC_TABDI
208
0
22523
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
x * 40000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A67Y
the mutation enhances the catalytic efficiency of the enzyme about 8fold while the thermostability of the mutant enzyme remains unchanged. The specific activity against azo-casein is almost 2.4 times higher than wild type
S32T
the mutation enhances the catalytic efficiency of the enzyme about 8fold while the thermostability of the mutant enzyme remains unchanged
S32T/A67Y
the mutations enhance the catalytic efficiency of the enzyme about 8fold while the thermostability of the mutant enzyme remains unchanged
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 80
after 10 incubation, the enzyme shows 100% activity between 40 and 55°C, about 97% activity at 60°C, about 65% activity at 70°C, 50% activity at 72°C, about 25% activity at 75°C, and no activity at 80°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dutta, S.; Dattagupta, J.K.; Biswas, S.
Enhancement of proteolytic activity of a thermostable papain-like protease by structure-based rational design
PLoS ONE
8
e62619
2013
Tabernaemontana divaricata (P83654), Tabernaemontana divaricata
Manually annotated by BRENDA team