Information on EC 3.4.21.90 - Togavirin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.90
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RECOMMENDED NAME
GeneOntology No.
Togavirin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-/-Ser- bond
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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serine endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY hide
37259-58-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Sindbis virus core protein + H2O
?
show the reaction diagram
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autocatalytic cleavage at Trp264, . Besides its catalytic activity it also plays important roles in the formation of the viral core, the recognition of the spike proteins during the budding process, the recognition and packaging of the viral RNA, and possibly the inhibition of the host cell protein synthesis
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Sindbis virus core protein + H2O
Hydrolyzed Sindbis core protein
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Sindbis virus core protein + H2O
?
show the reaction diagram
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autocatalytic cleavage at Trp264, . Besides its catalytic activity it also plays important roles in the formation of the viral core, the recognition of the spike proteins during the budding process, the recognition and packaging of the viral RNA, and possibly the inhibition of the host cell protein synthesis
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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in the host, the core protein is transferred to ribosomes, the ribosome bound core protein is distributed throughout the cytoplasm, whereas the genome RNA remains associated with vacuolar membranes
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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togavirin has a similar tertiary structure to chymotrypsin
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
at 25 A resolution
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at 9 A resolution, the C-terminal domain folds into a trypsin-like protease structure
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at 9 A resolution, the carboxyterminal domain folds into a trypsin-like protease structure
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
capsid protein(81-112) mutant, on Ni-agarose affinity column
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
peptide comprising amino acid residues 81 to 112 of the capsid protein expressed as an Smt3 fusion protein from a modified pET28b vector
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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alphavirus core protein is a target for antiviral chemotherapy
CDELTA(101-105)
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core accumulation, no encapsidation specificity
CDELTA(101-110)
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no core accumulation, no encapsidation specificity
CDELTA(106-110)
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no core accumulation, no encapsidation specificity
CDELTA(107-113)
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no core accumulation, no encapsidation specificity
CDELTA(91-100)
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no core accumulation, no encapsidation specificity
CDELTA(96-100)
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core accumulation, no encapsidation specificity
CDELTA(97-106)
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core accumulation, no encapsidation specificity
K102A
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stronger binding affinity for encapsidation signal RNA than the wild-type
K109A
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stronger binding affinity for encapsidation signal RNA than the wild-type
K83A
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binding affinity for encapsidation signal RNA comparable to the wild-type
K86A
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stronger binding affinity for encapsidation signal RNA than the wild-type
K92A
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weaker binding affinity for encapsidation signal RNA than the wild-type
K97A
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binding affinity for encapsidation signal RNA comparable to the wild-type
K97A/K99A
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10fold reduced binding affinity compared to that of the wild type
K99A
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weaker binding affinity for encapsidation signal RNA than the wild-type
K99E
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accumulates wild-type levels of nucleocapsid cores while still encapsidating approximately 65% viral RNA
K99E/R105A
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accumulates wild-type levels of nucleocapsid cores while still encapsidating approximately 65% viral RNA
K99L
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weaker binding affinity for encapsidation signal RNA than the wild-type
K99M
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stronger binding affinity for encapsidation signal RNA than the wild-type
K99R
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stronger binding affinity for encapsidation signal RNA than the wild-type
L108A
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stronger binding affinity for encapsidation signal RNA than the wild-type
L108D
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no core accumulation, no encapsidation specificity
L110A
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stronger binding affinity for encapsidation signal RNA than the wild-type
L110N
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no core accumulation, no encapsidation specificity
P100A
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weaker binding affinity for encapsidation signal RNA than the wild-type
Q104A
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binding affinity for encapsidation signal RNA comparable to the wild-type
Q88A
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weaker binding affinity for encapsidation signal RNA than the wild-type
Q94A
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binding affinity for encapsidation signal RNA comparable to the wild-type
R103A
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core accumulation, no encapsidation specificity
R103A/R105A
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100fold reduced binding affinity compared to that of the wild type
R105A
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core accumulation, no encapsidation specificity
R105E
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weaker binding affinity for encapsidation signal RNA than the wild-type
R105K
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stronger binding affinity for encapsidation signal RNA than the wild-type
R105L
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weaker binding affinity for encapsidation signal RNA than the wild-type
R105M
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weaker binding affinity for encapsidation signal RNA than the wild-type
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development