Information on EC 3.4.22.B15 - rabbit hemorrhagic disease virus 3C-like protease

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Rabbit hemorrhagic disease virus

EC NUMBER
COMMENTARY hide
3.4.22.B15
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
rabbit hemorrhagic disease virus 3C-like protease
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
the enzyme is responsible for cleavage at certain Q/G sites in the rabbit hemorrhagic disease virus polyprotein
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
37353-41-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Rabbit hemorrhagic disease virus polyprotein + H2O
?
show the reaction diagram
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
Rabbit hemorrhagic disease virus polyprotein + H2O
?
show the reaction diagram
-
cleavage sites: E718-G719, E1108-G1109, E1767-G1768 and E143-G144
-
-
?
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
upon expression in Escherichia coli, the protease releases itself from larger precursors by proteolytic cleavages at ist N and C termini. Cleavage at the N terminus of the protease occurs with low efficiency at E1108-G1109. Cleavage at the C terminus of the protease occurs with low efficiency at the E1251-T1252 bond
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
upon expression in Escherichia coli, the protease releases itself from larger precursors by proteolytic cleavages at its N and C termini. Cleavage at the N terminus of the protease occurs with low efficiency at E1108-G1109. Cleavage at the C terminus of the protease occurs with low efficiency at the E1251-T1252 bond
-