Information on EC 3.4.22.44 - nuclear-inclusion-a endopeptidase

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The expected taxonomic range for this enzyme is: Potyvirus

EC NUMBER
COMMENTARY
3.4.22.44
-
RECOMMENDED NAME
GeneOntology No.
nuclear-inclusion-a endopeptidase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Hydrolyses glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-/-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
49 kDa proteinase
-
-
-
-
49 kDa-Pro
-
-
-
-
NIA
-
-
-
-
NIa protease
-
-
-
-
NIa protease
turnip mosaic potyvirus
-
-
NIa protease
turnip mosaic potyvirus TuMV
-
-
-
NIa protease
-
-
NIa protein
Q708F7
-
NIa proteins
-
-
-
-
nuclear inclusion a protease
-
-
nuclear inclusion body protein a
-
-
-
-
nuclear inclusion protein A protease
-
-
-
-
nuclear inclusion protein-a protease
-
-
potyvirus NIa protease
-
-
-
-
protease NIa
-
-
-
-
proteinase Nia
-
-
-
-
proteinase, polyprotein-processing, Nia
-
-
-
-
proteins (specific proteins and subclasses), NIa (nuclear inclusion, a)
-
-
-
-
proteins NIa
-
-
-
-
proteins, small nuclear inclusion NIa
-
-
-
-
tobacco vein mottling virus protease
Q9J0W2
-
CAS REGISTRY NUMBER
COMMENTARY
139946-51-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
clover yellow vein virus ClYVV
ClYVV
-
-
Manually annotated by BRENDA team
Plum pox virus PPV
PPV
-
-
Manually annotated by BRENDA team
potato virus Y PVY
PVY
-
-
Manually annotated by BRENDA team
tobacco etch virus TEV
TEV
-
-
Manually annotated by BRENDA team
tobacco vein mottling virus TVMV
TVMV
-
-
Manually annotated by BRENDA team
turnip mosaic potyvirus
TuMV
-
-
Manually annotated by BRENDA team
turnip mosaic potyvirus TuMV
TuMV
-
-
Manually annotated by BRENDA team
polyprotein, part of the nuclear inclusion protein gene NIa of Vanilla mosaic virus-CI; VanMV, isolate from Vanilla tahitensis
SwissProt
Manually annotated by BRENDA team
zucchini yellow mosaic virus ZYMV
ZYMV
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
the nuclear inclusion a protease of turnip mosaic virus is responsible for the processing of the viral polyprotein into functional proteins. Degradation of Amyloid-beta in the cytoplasm can be a novel strategy to control the levels of Amyloid-beta, plaque formation, and the associated cell death
physiological function
Q9J0W2
the TVMV genome is translated into a single large polyprotein that is subsequently processed by three virally encoded proteases. Seven of the nine cleavage events are carried out by the NIa protease
additional information
-
overexpression of NIa in rat B103 neuroblastoma cells results in a significant reduction in cell death caused by both intracellularly generated and exogenously added Amyloidbeta. Moreover, lentiviral-mediated expression of NIa in APPsw/PS1 transgenic mice significantly reduces the levels of Amyloid-beta and plaques in the brain
additional information
-
the full-length potyviral genome protease, VPg-Pro, has two domains: an N-terminal viral protein genome-linked, VPg, and a C-terminal protease NIa-Pro. Regulation of nuclear inclusion protein-a protease is crucial for polyprotein processing and hence, for successful infection by potyviruses, mechanisms regulating nuclear inclusion protein-a protease activity. Firstly, the influence of the VPg domain on the proteolytic activity of NIa-Pro increases when the two domains interact each other. Secondly, the protease activity of NIa-Pro can also be modulated by phosphorylation at Ser129. interaction with VPg as well as phosphorylation of Ser129 relays a signal through Trp143 present at the protein surface to the active site pocket by subtle conformational changes, thus modulating protease activity of NIa-Pro, molecular modeling, homology modeling, and molecular dynamics simulations, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-Arg-Glu-Thr-Val-Arg-Phe-Gln-Ser-Asp-amide + H2O
?
show the reaction diagram
tobacco vein mottling virus, tobacco vein mottling virus TVMV
-
-
-
-
?
acetyl-Asn-Asn-Val-Arg-Phe-Gln-Ser-Leu-amide + H2O
acetyl-Asn-Asn-Val-Arg-Phe-Gln + Ser-Leu-amide
show the reaction diagram
tobacco vein mottling virus, tobacco vein mottling virus TVMV
-
-
-
?
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide + H2O
?
show the reaction diagram
turnip mosaic potyvirus
-
-
-
-
?
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide + H2O
?
show the reaction diagram
turnip mosaic potyvirus TuMV
-
-
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
-
-
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
-
-
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
turnip mosaic potyvirus
-
-
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
-
-
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
-
identification of cleavage site
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
-
analysis of cleavage sites, specific for its own polypeptide chain, no cleavage of other potyvirus NIa proteins
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
turnip mosaic potyvirus
-
the nuclear inclusion protein of potyviruses has two domains, the Vpg domain of 22 kDa and the C-terminal domain of 27 kDa which has proteolytic activity. The first cleavage at Ser223-Gly224 produces a 25 kDa protein. TuMV cleaves itself in cis, removing a 20 amino aicd peptide from the C-terminus. A second cleavage is very slow and occurs between Thr207-Ser208, resulting in a 24 kDa protein
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
Plum pox virus PPV
-
-
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
tobacco vein mottling virus TVMV
-
-
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
turnip mosaic potyvirus TuMV
-
the nuclear inclusion protein of potyviruses has two domains, the Vpg domain of 22 kDa and the C-terminal domain of 27 kDa which has proteolytic activity. The first cleavage at Ser223-Gly224 produces a 25 kDa protein. TuMV cleaves itself in cis, removing a 20 amino aicd peptide from the C-terminus. A second cleavage is very slow and occurs between Thr207-Ser208, resulting in a 24 kDa protein
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
turnip mosaic potyvirus TuMV
-
-
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
tobacco etch virus TEV
-
-
-
-
?
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln-Ser-Gly-Thr-Val-Asp-Arg-Arg + H2O
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln + Ser-Gly-Thr-Val-Asp-Arg-Arg
show the reaction diagram
tobacco etch virus, tobacco etch virus TEV
-
-
-
?
RETVRFQSD + H2O
?
show the reaction diagram
Q9J0W2
-
-
-
?
TETVRFQSGTRR + H2O
?
show the reaction diagram
Q9J0W2
-
-
-
?
turnip mosaic virus polyprotein + H2O
?
show the reaction diagram
turnip mosaic potyvirus, turnip mosaic potyvirus TuMV
-
cleaved at seven differnt locations
-
?
WDGGEVAHQAGESV + H2O
WDGGEVAHQ + AGESV
show the reaction diagram
-
-
-
-
?
amyloid-beta peptide + H2O
?
show the reaction diagram
-
degradation of oligomeric as well as monomeric forms of Amyloid-beta, presence of the consensus sequence, Val12-His-His-Gln15, near the presumptive alpha-secretase cleavage site of the amyloid-beta peptide
-
-
?
additional information
?
-
turnip mosaic potyvirus
-
consensus substrate sequence: Yaa-Val-Arg-His-Gln-/-Ser, with Yaa being a aliphatic amino acid and the scissile bond being located between Gln and Ser
-
?
additional information
?
-
-
interaction between purified recombinant NIa-Pro and VPg domains, overview
-
-
-
additional information
?
-
-
NIa possesses a relatively strict substrate specificity with a preference for Val-Xaa-His-GlnQ, with the scissile bond located after Gln
-
-
-
additional information
?
-
Q9J0W2
the S3 and S4 pockets are mainly responsible for the substrate specificity, comparison to the specificity of the tobacco etch virus, TEV, protease, structural determinants of substrate specificity, overview. The TVMV protease is less tolerant of variation at the P1' position than TEV protease, and substitutions in the P6 position are more readily tolerated by TVMV than TEV protease
-
-
-
additional information
?
-
turnip mosaic potyvirus TuMV
-
consensus substrate sequence: Yaa-Val-Arg-His-Gln-/-Ser, with Yaa being a aliphatic amino acid and the scissile bond being located between Gln and Ser
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nuclear inclusion protein a + H2O
?
show the reaction diagram
-
-
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
-
-
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
turnip mosaic potyvirus
-
-
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
-
-
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
-
identification of cleavage site
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
-
analysis of cleavage sites, specific for its own polypeptide chain, no cleavage of other potyvirus NIa proteins
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
turnip mosaic potyvirus
-
the nuclear inclusion protein of potyviruses has two domains, the Vpg domain of 22 kDa and the C-terminal domain of 27 kDa which has proteolytic activity. The first cleavage at Ser223-Gly224 produces a 25 kDa protein. TuMV cleaves itself in cis, removing a 20 amino aicd peptide from the C-terminus. A second cleavage is very slow and occurs between Thr207-Ser208, resulting in a 24 kDa protein
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
Plum pox virus PPV
-
-
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
tobacco vein mottling virus TVMV
-
-
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
turnip mosaic potyvirus TuMV
-
the nuclear inclusion protein of potyviruses has two domains, the Vpg domain of 22 kDa and the C-terminal domain of 27 kDa which has proteolytic activity. The first cleavage at Ser223-Gly224 produces a 25 kDa protein. TuMV cleaves itself in cis, removing a 20 amino aicd peptide from the C-terminus. A second cleavage is very slow and occurs between Thr207-Ser208, resulting in a 24 kDa protein
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
turnip mosaic potyvirus TuMV
-
-
-
-
?
nuclear inclusion protein a + H2O
?
show the reaction diagram
tobacco etch virus TEV
-
-
-
-
?
additional information
?
-
-
interaction between purified recombinant NIa-Pro and VPg domains, overview
-
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NEM
-
does not completely inhibit NIa activity
additional information
-
no competitive inhibition of the proteolytic activity by the presence of excess of different protease mutants
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.217
-
acetyl-Arg-Glu-Thr-Val-Arg-Phe-Gln-Ser-Asp-amide
-
-
-
0.216
-
acetyl-Asn-Asn-Val-Arg-Phe-Gln-Ser-Leu-amide
-
-
-
0.51
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 7.0, 12C
-
0.52
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 7.4, 12C
-
0.62
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 8.0, 12C
-
1.14
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 7.0, 25C
-
1.2
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 7.4, 25C
-
2.22
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease
-
2.64
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
25 kDa protease
-
2.83
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 8.0, 25C
-
0.069
-
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln-Ser-Gly-Thr-Val-Asp-Arg-Arg
-
27 kDa full length protease
0.271
-
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln-Ser-Gly-Thr-Val-Asp-Arg-Arg
-
truncated protease
0.082
-
TETVRFQSGTRR
Q9J0W2
recombinant wild-type TVMV protease, pH 7.0, 30C
-
0.108
-
TETVRFQSGTRR
Q9J0W2
recombinant mutant TVMV1-217 protease, pH 7.0, 30C
-
0.05
-
WDGGEVAHQAGESV
-
recombinant S129D NIa-Pro mutant, pH 8.5, 25C
-
0.06
-
WDGGEVAHQAGESV
-
recombinant S129A NIa-Pro mutant, pH 8.5, 25C
-
0.15
-
WDGGEVAHQAGESV
-
recombinant S129D NIa-Pro mutant in presence of the VPg domain, pH 8.5, 25C
-
0.44
-
WDGGEVAHQAGESV
-
recombinant wild-type NIa-Pro, pH 8.5, 25C
-
0.45
-
WDGGEVAHQAGESV
-
recombinant E191A VPg-Pro mutant, pH 8.5, 25C
-
0.69
-
WDGGEVAHQAGESV
-
recombinant W143A NIa-Pro mutant, pH 8.5, 25C
-
1.67
-
WDGGEVAHQAGESV
-
recombinant VPg-Pro, pH 8.5, 25C
-
11.4
-
WDGGEVAHQAGESV
-
recombinant W143A NIa-Pro mutant in presence of the VPg domain, pH 8.5, 25C
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.079
-
acetyl-Arg-Glu-Thr-Val-Arg-Phe-Gln-Ser-Asp-amide
-
-
-
0.071
-
acetyl-Asn-Asn-Val-Arg-Phe-Gln-Ser-Leu-amide
-
-
-
0.12
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 7.0, 12C
-
0.19
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 7.0, 25C
-
0.22
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 7.4, 12C
-
0.32
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease
-
0.33
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
25 kDa protease
-
0.34
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 7.4, 25C
-
0.373
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 8.0, 12C
-
1.01
-
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 8.0, 25C
-
0.033
-
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln-Ser-Gly-Thr-Val-Asp-Arg-Arg
-
truncated protease
0.18
-
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln-Ser-Gly-Thr-Val-Asp-Arg-Arg
-
27 kDa full length protease
0.092
-
TETVRFQSGTRR
Q9J0W2
recombinant wild-type TVMV protease, pH 7.0, 30C
-
0.094
-
TETVRFQSGTRR
Q9J0W2
recombinant mutant TVMV1-217 protease, pH 7.0, 30C
-
0.002
-
WDGGEVAHQAGESV
-
recombinant W143A NIa-Pro mutant, pH 8.5, 25C
-
0.004
-
WDGGEVAHQAGESV
-
recombinant S129D NIa-Pro mutant, pH 8.5, 25C
-
0.005
-
WDGGEVAHQAGESV
-
recombinant S129A NIa-Pro mutant, pH 8.5, 25C
-
0.006
-
WDGGEVAHQAGESV
-
recombinant S129D NIa-Pro mutant in presence of the VPg domain, pH 8.5, 25C
-
0.01
-
WDGGEVAHQAGESV
-
recombinant W143A NIa-Pro mutant in presence of the VPg domain, pH 8.5, 25C
-
0.034
-
WDGGEVAHQAGESV
-
recombinant wild-type NIa-Pro, pH 8.5, 25C
-
0.063
-
WDGGEVAHQAGESV
-
recombinant E191A VPg-Pro mutant, pH 8.5, 25C
-
0.23
-
WDGGEVAHQAGESV
-
recombinant VPg-Pro, pH 8.5, 25C
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.87
-
TETVRFQSGTRR
Q9J0W2
recombinant mutant TVMV1-217 protease, pH 7.0, 30C
0
1.12
-
TETVRFQSGTRR
Q9J0W2
recombinant wild-type TVMV protease, pH 7.0, 30C
0
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
Q708F7
amino acid and nucleotide identity percentages across the whole coat protein shown, the coat protein core region and the 3' non-translated region indicated, sequence identity to several Potyvirus strains determined, phylogenetic tree analysis performed
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
Q9J0W2
assay at
7.4
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
-
turnip mosaic potyvirus
-
temperature optimum for the 24 kDa protein
15
-
turnip mosaic potyvirus
-
temperature optimum of the 27 kDa full length protease. The optimum is not related to the C-terminal cleavage site but to the stability or flexibility of the structure of the NIa protease
25
-
-
assay at
30
-
Q9J0W2
assay at
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23000
-
-
mass spectrometry, N-terminal amino acid sequence
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
Q9J0W2
three-dimensional structure of TVMV protease, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
the protease activity of NIa-Pro can be modulated by phosphorylation at Ser129
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified recombinant mutant TVMV protease K65A/K67A/C151A in complex with a canonical peptide substrate RETVRFQSD, mixing of protein solution with 10 mg/ml protein with a fivefold molar excess of the peptide substrate RETVRFQSD, crystallization from a solution consisting of 0.2 M potassium formate and 20% PEG 3350, space group P212121, X-ray diffraction structure determination and analysis at 1.7 A resolution, the 20-residue C-terminus of TVMV protease is disordered, molecular replacement, using the crystal structure of TEV protease, PDB code 1Q31
Q9J0W2
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
-
turnip mosaic potyvirus
-
instable above
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gel filtration
Q708F7
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
co-expression of NIa-Pro and Vg-Pro in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Q9J0W2
cloning of NIa in Escherichia coli, overexpression of HA-tagged NIa in rat B103 neuroblastoma cells
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C151A
-
site-directed mutagenesis, a NIa-Pro active site mutant
E191A
-
site-directed mutagenesis, a VPg-Pro mutant
S129A
-
site-directed mutagenesis, a NIa-Pro phosphorylation-deficient mutant
S129D
-
site-directed mutagenesis, a NIa-Pro phosphorylation-mimic mnutant
W143A
-
site-directed mutagenesis, the NIa-Pro W143A mutant can bind the substrate with almost equal affinity as that of the wild-type protease, although its ability to catalyze the cleavage reaction is highly reduced
E189L
-
no self-cleavage
C151A
Q9J0W2
catalytically inactive mutant TVMV protease
K65A/K67A/C151A
Q9J0W2
catalytically inactive mutant TVMV protease
additional information
Q9J0W2
a truncation mutant of TVMV protease lacking the 20 C-terminal amino acid residues, TVMV1-217 protease, shows reduced activity compared to the wild-type enzyme
G224R
turnip mosaic potyvirus
-
almost no self-cleavage of the 25 kDa protein
additional information
turnip mosaic potyvirus
-
comparison of the catalytic activities of wild-type, mutant and C-terminal truncated proteases
G224R
turnip mosaic potyvirus TuMV
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almost no self-cleavage of the 25 kDa protein
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additional information
turnip mosaic potyvirus TuMV
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comparison of the catalytic activities of wild-type, mutant and C-terminal truncated proteases
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additional information
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overexpression of HA-tagged NIa in rat B103 neuroblastoma cells and lentiviral-mediated expression of NIa in APPsw/PS1 transgenic mice or human 293T cells, the pattern of NIa expression shows a wide distribution throughout the mouse brain including the cerebral cortex, hippocampus, amygdala, and thalamus, and the Amyloid-beta deposition in the prefrontal cortex, parietal cortex, hippocampus and piriform cortex is remarkably decreased in the brain infused with Lenti-NIa in comparison to the brain infused with Lenti-GFP. Expression of wild-type and utant, with an Asp to Ala substitution in the catalytic triad,.Amyloid-beta intracellularly in B103 cells using the plasmid pGFPUb-Abeta, encoding a triple fusion protein of green fluorescent protein, ubiquitin, and Amylod-beta. The peptide bond between ubiquitin and Amyloid-beta is cleaved quickly by endogenous deubiquitinating enzymes, generating an equimolar ratio of GFP-ubiquitin and Amyloid-beta in the cytosol
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
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induction of pathogen derived resistance to plant viruses
agriculture
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plants transformed with a NIa cistron show a high degree of resistance to potato virus Y
agriculture
potato virus Y PVY
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induction of pathogen derived resistance to plant viruses
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agriculture
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induction of pathogen derived resistance to plant viruses
agriculture
tobacco etch virus TEV
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induction of pathogen derived resistance to plant viruses
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agriculture
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induction of pathogen derived resistance to plant viruses
agriculture
tobacco vein mottling virus TVMV
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induction of pathogen derived resistance to plant viruses
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