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.

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 proteases, 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

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.B50 papain-like proteinase 2

Engineering

Engineering on EC 3.4.22.B50 - papain-like proteinase 2

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C1651A
C1732A
-
encodes a substitution of a cysteine residue, predicted to be critical for zinc binding
D1826A
-
purified SARS-CoV PLpro protein containing an alanine substitution at putative catalytic residues
C1651A
-
Plpro active-site mutant; purified SARS-CoV PLpro protein containing an alanine substitution at putative catalytic residues
-
C1732A
-
encodes a substitution of a cysteine residue, predicted to be critical for zinc binding
-
D1826A
-
purified SARS-CoV PLpro protein containing an alanine substitution at putative catalytic residues
-
C270A/H332A
active site mutant
I353R
the mutant exhibits about 40fold reduction in specificity toward ubiquitin compared to the wild type while the activity toward RLRGG-7-amido-4-methylcoumarin is essentially unaltered
I353W
the mutant exhibits about 10fold reduction in specificity toward ubiquitin compared to the wild type while the activity toward RLRGG-7-amido-4-methylcoumarin is essentially unaltered
T312A/I313V/I353R
the mutant shows the greatest decrease in inhibitory activity in the interferon-beta promoter activity assay
C106A
-
inactive
C1729A
the mutant shows reduced interferon antagonistic activity compared to that of the wild type enzyme
D1901A
the mutant almost completely loses interferon antagonistic activity compared to that of the wild type enzyme
H1888A
the mutant almost completely loses interferon antagonistic activity compared to that of the wild type enzyme
D165A
site-directed mutagenesis, the mutant shows reduced activity in deubiquitination compared to the wild-type enzyme
E168A
site-directed mutagenesis, the mutant shows reduced activity in deubiquitination compared to the wild-type enzyme
E168D
site-directed mutagenesis, the mutant shows reduced activity in deubiquitination compared to the wild-type enzyme
E168R
site-directed mutagenesis, the mutant shows reduced activity in deubiquitination compared to the wild-type enzyme
L163Q
site-directed mutagenesis, the mutant shows reduced activity in deubiquitination compared to the wild-type enzyme
Y265A
site-directed mutagenesis, the mutant shows reduced activity in deubiquitination compared to the wild-type enzyme
Y265F
site-directed mutagenesis, the mutant shows reduced activity in deubiquitination compared to the wild-type enzyme
Y274A
site-directed mutagenesis, inactive mutant
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