3.4.21.113: pestivirus NS3 polyprotein peptidase
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For detailed information about pestivirus NS3 polyprotein peptidase, go to the full flat file.
Word Map on EC 3.4.21.113
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3.4.21.113
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polyproteins
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dengue
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cytopathogenic
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bluetongue
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ns4a
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ntpase
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flaviviruses
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flaviviridae
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horsesickness
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pestiviruses
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drug development
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medicine
- 3.4.21.113
- polyproteins
- dengue
-
cytopathogenic
-
bluetongue
- ns4a
- ntpase
- flaviviruses
- flaviviridae
- horsesickness
- pestiviruses
- drug development
- medicine
Reaction
Leu is conserved at position P1 for all four cleavage sites. Alanine is found at position P1' of the NS4A-NS4B cleavage site, whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A and NS5A-NS5B cleavage sites =
Synonyms
border disease virus NS3 endopeptidase, BVD NS3 endopeptidase, BVDV NS3 endopeptidase, classical swine fever virus NS3 endopeptidase, CSFV NS3, CSFV NS3 endopeptidase, flavivirus NS3 protease, nonstructural protein 3, nonstructural protein NS3, NS2B/NS3 protease, NS3, NS3 protease, NS3 protein, NS3 proteinase, NS3 serine protease, NS3-4A protease, NS3-SP, NS3prohelx, P80pestivirus P80 protein, pestivirus NS3 protease, S31.001, viral diarrhea virus endopeptidase, WNV NS2B/NS3
ECTree
3.4.21.113 pestivirus NS3 polyprotein peptidaseAdvanced search results
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results (Engineering
Engineering on EC 3.4.21.113 - pestivirus NS3 polyprotein peptidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D1686G
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mutation does not induce obvious changes in processing
D1695A
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mutation does not induce obvious changes in processing
S1752C
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mutant enzyme exhibits only cleavage activity at the NS3/4A site
S1752T
K232A
site-directed mutagenesis, helicase active site mutant
S163A
site-directed mutagenesis, protease active site mutant, proteolytically inactive
V132A
mutation of residue 132 of the NS3 protease domain, the gain of function mutation in NS3 maps to a hydrophobic surface patch which interacts with the NS4A-kink region
K48A
to prevent its self-cleavage an autolytic site-deficient mutant is generated
additional information
S1752T
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mutant enzyme exhibits only cleavage activity at the NS3/4A site
additional information
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the NS3 protease is sensitive to N-terminal truncation because a deletion of 6 amino acids significantly reduces the cleavage efficiency at the NS4A/4B site
additional information
construction of recombinant full-length NS3 (residues 1 to 683) followed by the 8 N-terminal residues of NS4A, the NS3 sequence is preceeded by residues 21 to 57 of the protease cofactor NS4A
additional information
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protease deletion constructs of the helicase domain NS3hel(deltaN166) and NS3hel(deltaN188), which are missing 166 and 188 amino acids, respectively, from the N-terminus of the NS3 protein. NS3hel(deltaN188) binds TS34 RNA, RNA binding by NS3hel(deltaN166) is not detectable
additional information
it is shown that both NS3 helicase and NS3 proteinase-helicase constructs are capable of unwinding both the DNA and the RNA templates. In contrast, the full-length NS2B-NS3 proteinase-helicase unwinds only the RNA templates, whereas its DNA unwinding activity is severely repressed
additional information
using a construct consisting of the upstram NS2B sequence and the proteinase domain bearing a K48A mutation followed by the helicase domain and another constrcut lacking the helicase domain it is shown that the helicase domain does not significantly affect the proteolytic activity
