3.4.22.46: L-peptidase

This is an abbreviated version!
For detailed information about L-peptidase, go to the full flat file.

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 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.22 Cysteine endopeptidases

                3.4.22.46 L-peptidase

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Results	in table
15	AA Sequence
1	Application
1	CAS Registry Number
18	Cloned(Commentary)
4	Crystallization (Commentary)
11	General Information
11	Inhibitors
6	Ki Value [mM]
1	KM Value [mM]
2	Localization
11	Molecular Weight [Da]
35	Natural Substrates/ Products (Substrates)
40	Organism
26	PDB ID
4	pH Optimum
1	pH Range
2	Posttranslational Modification
26	Protein Variants
8	Purification (Commentary)
1	Reaction
1	Reaction Type
33	Reference
1	Source Tissue
1	Specific Activity [micromol/min/mg]
1	Storage Stability
62	Substrates and Products (Substrate)
9	Subunits
67	Synonyms
3	Temperature Optimum [°C]

General Information

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General Information on EC 3.4.22.46 - L-peptidase

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

evolution

Foot-and-mouth disease virus

-

significant conformational adaptation by the enzyme is important for substrate recognition, specificity differences between 3Cpro from different picornaviruses, overview

709535

malfunction

2 entries

metabolism

Lactococcus lactis

D9IXC0

functions in the last step of nisin maturation as the leader-peptide peptidase

731065

physiological function

6 entries

additional information

Citrus tristeza virus

-

the region encoding leader proteases plays a role in the superinfection exclusion (SIE), a phenomenon in which a primary virus infection prevents a secondary infection with the same or closely related virus

755647

malfunction

Mycobacterium tuberculosis

P9WKA1

the inhibition of LepB results in repressing the cleavage of the signal peptide from the preproteins which would lead to arresting the folding of proteins which are essential for the growth and pathogenesis of Mycobacterium tuberculosis into their active mature conformation

731252

malfunction

Mycobacterium tuberculosis H37Rv

-

the inhibition of LepB results in repressing the cleavage of the signal peptide from the preproteins which would lead to arresting the folding of proteins which are essential for the growth and pathogenesis of Mycobacterium tuberculosis into their active mature conformation

-

physiological function

Foot-and-mouth disease virus

-

foot and mouth disease virus expresses its genetic information as a single polyprotein that is translated from the single-stranded RNA genome. The leader protease, Lbpro, performs the initial cleavage by freeing itself from the growing polypeptide chain. Subsequently, Lbpro cleaves the two homologues of the host cell protein eukaryotic initiation factor 4G, eIF4G. Lbpro possesses specific binding sites at the non-prime side from S1 down to S7

717297

physiological function

Foot-and-mouth disease virus

-

the leader proteinase, Lpro, acts as an interferon-beta antagonist and inhibits IFN-alpha1/beta promoter activation, poly(I:C)-induced IFN-alpha1/beta mRNA expression, and dsRNA-induced type I interferon transcription by decreasing interferon regulatory factor 3/7 in protein levels. Lpro significantly reduced the transcription of multiple IRF-responsive genes

717188

physiological function

Foot-and-mouth disease virus

-

the viral RNA genome is translated in the cytoplasm of infected cells as a long polyprotein precursor that is cleaved by virally encoded proteases to release functional proteins needed for the synthesis of new virions. In 10 of 13 cases, 3Cpro performs the cleavages by targeting specific sequences within the polyprotein

709535

physiological function

cucumber vein yellowing virus

Q1G2C1

host-dependent separation of the enzyme from the remainder of the polyprotein is essential for suppressing RNA silencing defenses and for efficient viral infection

732976

physiological function

Foot-and-mouth disease virus

-

the enzyme inhibits the host innate immune response by the revention of the synthesis of cytokines such as interferons immediately after infection (brought about by specific proteolytic cleavage of the eukaryotic initiation factor 4G) as well as nuclear factor-kappaB cleavage and the deubiquitination of immune signalling molecules

731405

physiological function

Foot-and-mouth disease virus

-

LGP2 cleavage by the Leader protease of aphthoviruses may represent an antagonistic mechanism for immune evasion

755214