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
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serotypes
- coxsackievirus
- vp3
- picornaviridae
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encephalomyocarditis
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papain-like
- rupintrivir
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3c-like
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poliovirus-infected
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anti-ev71
-
cloven-hoofed
-
coxsackie
-
fmdv-infected
- aphthovirus
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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 (Natural Substrates Products
Natural Substrates Products on EC 3.4.22.46 - L-peptidase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
eukaryotic initiation factor 4G + H2O
?
-
Lbpro cleaves two homologues of the host cell protein. Lbpro possesses specific binding sites at the non-prime side from S1 down to S7
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-
?
nisin + H2O
?
the final step in nisin maturation is the proteolytic cleavage of the first 23 amino-terminal residues by NisP
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-
?
nisin-(leader peptide) + H2O
nisin + leader peptide
after translocation into the extracellular space, the leader peptide is cleaved by the leader peptidase NisP, resulting in active nisin. NisP recognizes the cleavage site GASPR-/-IT located at the C-terminal end of the leader peptide
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-
?
RNA helicase LGP2 + H2O
?
-
LGP2 cleavage by the Leader protease of aphthoviruses may represent an antagonistic mechanism for immune evasion
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-
?
eukaryotic initiation factor eIF4G + H2O
?
in intermolecular cleavage on polyprotein substrates, isoform Lbpro is unaffected by P1 or P1' substitutions and processes a substrate containing nine eIF4GI cleavage site residues whereas isoform sLbpro fails to cleave the eIF4GI containing substrate and cleaves appreciably more slowly on mutated substrates
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-
?
eukaryotic initiation factor eIF4G + H2O
?
-
-
-
-
?
eukaryotic initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage prevents the synthesis of host cellular protein from capped cellular mRNAs, while the viral RNA is tsill translated initiating from an internal ribosome entry site
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-
?
eukaryotic initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, recognition/cleavage site is ANLG*RTTL
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-
?
eukaryotic initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, recognition/cleavage site is ANLG*RTTL
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-
?
eukaryotic initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage prevents the synthesis of host cellular protein from capped cellular mRNAs, while the viral RNA is tsill translated initiating from an internal ribosome entry site
-
-
?
eukaryotic initiation factor eIF4GII + H2O
?
-
eukaryotic host cell protein substrate, cleavage prevents the synthesis of host cellular protein from capped cellular mRNAs, while the viral RNA is tsill translated initiating from an internal ribosome entry site
-
-
?
eukaryotic initiation factor eIF4GII + H2O
?
-
eukaryotic host cell protein substrate, recognition/cleavage site is LNVG*SRRS, but not ADFG*RQTP
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-
?
eukaryotic initiation factor eIF4GII + H2O
?
-
eukaryotic host cell protein substrate, recognition/cleavage site is LNVG*SRRS, but not ADFG*RQTP
-
-
?
eukaryotic initiation factor eIF4GII + H2O
?
-
eukaryotic host cell protein substrate, cleavage prevents the synthesis of host cellular protein from capped cellular mRNAs, while the viral RNA is tsill translated initiating from an internal ribosome entry site
-
-
?
eukaryotic translation initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage causes the rapid inhibition of cellular cap-dependent protein synthesis
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-
?
eukaryotic translation initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage causes the rapid inhibition of cellular cap-dependent protien synthesis
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-
?
eukaryotic translation initiation factor eIF4GI + H2O
?
-
eukaryotic host cell protein substrate, cleavage causes the rapid inhibition of cellular cap-dependent protein synthesis
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-
?
foot-and-mouth disease leader protein + H2O
?
-
cis and trans cleavage activity at the L/P1 junction
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-
?
foot-and-mouth disease leader protein + H2O
?
-
similar to other papain-like proteinases the enzyme possesses the catalytic cysteine and histidine residues, however the catalytic asparagine has been replaced by an aspartate. The interaction between the histidine and aspartate is exposed to solvent, as the tryptophan residues are missing. The cleavage site is between its own C-terminus and the N-terminus of VP4
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-
?
additional information
?
-
-
the enzyme inhibits the immediate-early induction of beta interferon mRNA and blocks the host innate immune response by inhibition of IFN-induction of double-stranded RNA-dependent protein kinase R, 2',5'-oligoadenylate synthase, and Mx1 mRNAs in host porcine cells
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-
?
additional information
?
-
-
the leader protease, Lbpro, performs the initial cleavage by freeing itself from the growing polypeptide chain. Lbpro is not only one of the smallest papain-like cysteine peptidases but also one of the most specific. It has high prime side specificity at least down to the S' 5 site. It can still however cleave between both K-G and G-R pairs
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-
?
additional information
?
-
-
the enzyme cleaves itself off the nascent viral polyprotein
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-
?
additional information
?
-
-
the enzyme inhibits the immediate-early induction of beta interferon mRNA and blocks the host innate immune response by inhibition of IFN-induction of double-stranded RNA-dependent protein kinase R, 2',5'-oligoadenylate synthase, and Mx1 mRNAs in host porcine cells
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-
?
additional information
?
-
the enzyme possesses an auto-cleavage site between residues Arg647 and Ser648
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-
?
additional information
?
-
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the enzyme possesses an auto-cleavage site between residues Arg647 and Ser648
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-
?
translation initiation factor eIF4G + H2O
additional information
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-
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-
-
?
translation initiation factor eIF4G + H2O
additional information
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-
-
-
-
?
translation initiation factor eIF4G + H2O
additional information
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-
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-
-
?
translation initiation factor eIF4G + H2O
additional information
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-
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characterization of cleavage products, primary cleavage of rabbit reticulocyte eIF-4-gamma occurs between Gly479-Arg480, complete proteolysis after 12 h
?
translation initiation factor eIF4G + H2O
additional information
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very rapid reaction
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-
?
translation initiation factor eIF4G + H2O
additional information
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i.e. p220
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-
?
