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Information on EC 3.4.22.66 - calicivirin and Organism(s) Feline calicivirus and UniProt Accession Q66914

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.66 calicivirin
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This record set is specific for:
Feline calicivirus
UNIPROT: Q66914 not found.
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The taxonomic range for the selected organisms is: Feline calicivirus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-/- and the P1' position is occupied by Gly-/-
Synonyms
3clpro, 3c-like protease, 3c-like proteinase, 3c-like cysteine protease, 3cl pro, nv protease, nv 3clpro, virus-encoded 3c-like proteinase, calicivirus protease, 3c-like viral protease, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3C-like proteinase
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3C-like viral protease
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-
-
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3Cpro
-
-
-
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C37.001
-
-
-
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calicivirus protease
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Southampton virus 3C-like protease
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
218925-73-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Poly(A)-binding protein + H2O
?
show the reaction diagram
cleavage separates the C-terminal domain of the substrate that binds translation factors eIF4B and eRF3 from the N-terminal RNA-binding domain
-
-
?
F4 capsid precursor protein + H2O
?
show the reaction diagram
-
-
-
-
?
F4 NS6-7 protein + H2O
?
show the reaction diagram
-
strain F4 protein containing protease and RNA-dependent RNA-polymerase region
-
-
?
FRLEADDG + H2O
FRLE + ADDG
show the reaction diagram
-
-
-
-
?
additional information
?
-
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four amino acid residues are essential to protease activities: H39, E60, C122, and H137. These amino acids are involved in the formation of a conserved catalytic surface
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,6-di(propan-2-yl)-N-(4-[[4-(prop-2-en-1-yl)-5-sulfanylidene-4,5-dihydro-1H-1,2,4-triazol-3-yl]methyl]-1,3-thiazol-2-yl)-1H-pyrazolo[3,4-b]pyridine-4-carboxamide
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compound is predicted to bind to feline calicivirus proteases in a mode similar to that of the authentic substrate, and has the ability to inhibit viral protease activity in vitro and in the cells, and to suppress viral replication in FCV-infected cells. The authentic substrate and anti-FCV compound share a highly conserved binding site
benzyl [(2S)-1-[[(2S)-3-methyl-1-oxo-1-([(2S)-1-oxo-3-[(1S)-2-oxocyclopentyl]propan-2-yl]amino)butan-2-yl]amino]-3-(naphthalen-1-yl)-1-oxopropan-2-yl]carbamate
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tripeptidyl compound, potent antiviral activities against both feline coronavirus strain WSU-79-1146 and feline calicivirus strain Urbana. Treatment of coronavirus-infected mice with the compound at 100 mg/kg results in a significant reduction in liver virus titers
N2-[(benzyloxy)carbonyl]-N-[(2S)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]-1-(sulfinooxy)propan-2-yl]-L-valinamide
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dipeptidyl compound, statistically significant reduction in the viral load in the liver of virus-infected mice is consistently observed
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
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acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular model of the protease bound with octapeptide FRLEADDG containing a cleavage site of the capsid precursor protein
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C122S
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site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
additional information
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acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kuyumcu-Martinez, M.; Belliot, G.; Sosnovtsev, S.V.; Chang, K.O.; Green, K.Y.; Lloyd, R.E.
Calicivirus 3C-like proteinase inhibits cellular translation by cleavage of poly(A)-binding protein
J. Virol.
78
8172-8182
2004
Enterovirus C, norovirus, feline calicivirus (Q66914), feline calicivirus, norovirus MD145-12
Manually annotated by BRENDA team
Oka, T.; Yamamoto, M.; Yokoyama, M.; Ogawa, S.; Hansman, G.S.; Katayama, K.; Miyashita, K.; Takagi, H.; Tohya, Y.; Sato, H.; Takeda, N.
Highly conserved configuration of catalytic amino acid residues among calicivirus-encoded proteases
J. Virol.
81
6798-6806
2007
feline calicivirus, Sapovirus
Manually annotated by BRENDA team
Oka, T.; Murakami, K.; Wakita, T.; Katayama, K.
Comparative site-directed mutagenesis in the catalytic amino acid triad in Calicivirus proteases
Microbiol. Immunol.
55
108-114
2011
Rabbit hemorrhagic disease virus, Norwalk virus, feline calicivirus, Sapporo virus
Manually annotated by BRENDA team
Yokoyama, M.; Oka, T.; Takagi, H.; Kojima, H.; Okabe, T.; Nagano, T.; Tohya, Y.; Sato, H.
A proposal for a structural model of the feline calicivirus protease bound to the substrate peptide under physiological conditions
Front. Microbiol.
8
1383
2017
feline calicivirus, feline calicivirus F4
Manually annotated by BRENDA team
Kim, Y.; Shivanna, V.; Narayanan, S.; Prior, A.M.; Weerasekara, S.; Hua, D.H.; Kankanamalage, A.C.; Groutas, W.C.; Chang, K.O.
Broad-spectrum inhibitors against 3C-like proteases of feline coronaviruses and feline caliciviruses
J. Virol.
89
4942-4950
2015
feline calicivirus, feline coronavirus, feline calicivirus Urbana, feline coronavirus FIPV WSU-79/1146
Manually annotated by BRENDA team
Wu, H.; Zu, S.; Sun, X.; Liu, Y.; Tian, J.; Qu, L.
N-Terminal domain of feline calicivirus (FCV) proteinase-polymerase contributes to the inhibition of host cell transcription
Viruses
8
E199
2016
feline calicivirus, feline calicivirus (P27409), feline calicivirus 2280, feline calicivirus F9 (P27409)
Manually annotated by BRENDA team