3.4.22.46: L-peptidase
This is an abbreviated version!
For detailed information about L-peptidase, go to the full flat file.
Word Map on EC 3.4.22.46
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3.4.22.46
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polyproteins
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viruses
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enterovirus
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rhinovirus
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capsid
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poliovirus
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picornavirus
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serotypes
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coxsackievirus
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vp3
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picornaviridae
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encephalomyocarditis
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papain-like
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rupintrivir
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3c-like
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poliovirus-infected
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anti-ev71
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cloven-hoofed
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coxsackie
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fmdv-infected
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aphthovirus
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seneca
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3clpro
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drug development
- 3.4.22.46
- polyproteins
- viruses
- enterovirus
- rhinovirus
-
capsid
- poliovirus
- picornavirus
-
serotypes
- coxsackievirus
- vp3
- picornaviridae
-
encephalomyocarditis
-
papain-like
- rupintrivir
-
3c-like
-
poliovirus-infected
-
anti-ev71
-
cloven-hoofed
-
coxsackie
-
fmdv-infected
- aphthovirus
-
seneca
- 3clpro
- drug development
Reaction
autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-/-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-/-Arg- and -Lys-/-Arg- =
Synonyms
3C protease, 3Cpro, Eukaryotic signal peptidase, Eukaryotic signal proteinase, FMDV 3Cpro, foot-and-mouth disease virus 3C protease, L protein, L proteinase, Lab protein, Lb proC, Lbpro, Leader peptidase, leader peptidase B, leader peptidase NisP, Leader peptide hydrolase, leader protease, Leader proteinase, leaderprotease L1, leaderprotease L2, LepB, Lpro, nisin leader peptidase, NisP, nsp1alpha, P1a protein, Peptidase, signal, Prokaryotic leader peptidase, Prokaryotic signal peptidase, Prokaryotic signal proteinase, Propeptidase, Proteinase, eukaryotic signal, Proteinase, signal, Signal peptidase, Signalase, sLbpro
ECTree
3.4.22.46 L-peptidaseAdvanced search results
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results (Engineering
Engineering on EC 3.4.22.46 - L-peptidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C95K/C142L/C163A
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the C-terminally truncated, catalytically inactive mutant has wild-type binding activity but remains soluble at purified protein concentrations in excess of 10 mg/ml
C95K/C142S/C163A
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C-terminally truncated, catalytically inactive form of the type A10FMDV 3Cpro
L143A
self-processes efficiently at the L(pro)/VP4 cleavage site containing P2 phenylalanine, self-processing at the eIF4GII sequence Asp-Phe-Gly-Arg-Gln-Thr is improved but shows more-extensive aberrant processing
L143M
does not self-process efficiently at the L(pro)/VP4 cleavage site containing P2 phenylalanine
L200F
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the mutant is impaired in but still allows self-processing
R647P/S648P
the mutant has full catalytic activity for nisin leader-peptide cleavage, although the C-terminal region of the enzyme is no longer cleaved
L200F
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the mutant is impaired in activity but still allows self-processing
additional information
additional information
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a mutant virus A12-LLV2 lacking the leader proteinase is attenuated in cell culture and susceptible animals due to the inability of the mutant virus to block the expression of type I interferon alpha/beta, the blockade results in the IFN-induced inhibition of FMDV replication, overview
additional information
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mutation of the viral polyprotein self-processing cleavage site QRKLK*GAGQ, replacement by several variants of the two protein substrate elIF4G cleavage sites ANLG*RTTL and LNVG*SRRS, overview
additional information
leader proteinase self-processes inefficiently at the L(pro)/VP4 cleavage site Lys-Leu-Lys-Gly-Ala-Gly when the leucine at position P2 is replaced by phenylalanine: Molecular modeling and energy minimization identifies the L(pro) residue L143 as being responsible for this discrimination
additional information
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Lpro regulates the activity of nuclear factor kappa B. Analysis of NF-kappa B-dependent reporter gene expression in BHK-21 cells (baby hamster kidney cells strain 21), demonstrate that infection with wild-type virus has an inhibitory effect compared to infection with a genetically engineered mutant (A12-LLV2) lacking the leader coding region
additional information
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introduction of FLAG- and HA-tag on the small tetracysteine tc motif CCGPCC of cDNA-derived mutant FMDV A24-L1123, the mutant shows a small plaque phenotype similar to the parental A24-L1123 mutant. Expression of the Flag- or tc-tagged Lab protein is abolished or greatly diminished in these viruses. The A24-L1123/Flag virus acquires an extra base in the inter-AUG region that results in new AUG codons in-frame with the second AUG, and produced a larger Lb protein. This N-terminal extension of the Lb protein in mutant A24-L1123/Flag does not affect virus viability or L functions in cell culture
additional information
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mutation of the viral polyprotein self-processing cleavage site QRKLK*GAGQ, replacement by several variants of the two protein substrate elIF4G cleavage sites ANLG*RTTL and LNVG*SRRS, overview
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additional information
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a mutant virus A12-LLV2 lacking the leader proteinase is attenuated in cell culture and susceptible animals due to the inability of the mutant virus to block the expression of type I interferon alpha/beta, the blockade results in the IFN-induced inhibition of FMDV replication, overview
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