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Information on EC 3.4.21.91 - Flavivirin and Organism(s) Japanese encephalitis virus and UniProt Accession P27395

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.91 Flavivirin
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This record set is specific for:
Japanese encephalitis virus
UNIPROT: P27395 not found.
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Word Map
The taxonomic range for the selected organisms is: Japanese encephalitis virus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Selective hydrolysis of -Xaa-Xaa-/-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala
Synonyms
ns3 protease, nonstructural protein 3, ns2b-ns3 protease, ns3 serine protease, ns2b-ns3pro, ns2b/ns3 protease, ns3 proteinase, ns3pro, ns2b/ns3, zikv protease, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NS2B-NS3 protease-helicase
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NS2B-3 proteinase
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-
-
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NS2B-NS3 protease
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Yellow fever virus (flavivirus) protease
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CAS REGISTRY NUMBER
COMMENTARY hide
154215-26-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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interaction of human brain proteins with the Japanese encephalitis virus NS2B-NS3 protease could be involved in the Japanese encephalitis virus induced pathogenesis
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NS2B cofactor
N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease
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NS2B protein
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
enzyme ligand binding structure analysis
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
genome polyprotein; JEV
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of enzyme structure, PDB ID 2Z83
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
NS2B-NS3 protease
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
plasmid pJEVNS2B40-G4SG4-ASR-NS3FL expressed in Escherichia coli strain Rosetta2
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lin, C.W.; Lin, K.H.; Lyu, P.C.; Chen, W.J.
Japanese encephalitis virus NS2B-NS3 protease binding to phage-displayed human brain proteins with the domain of trypsin inhibitor and basic region leucine zipper
Virus Res.
116
106-113
2006
Japanese encephalitis virus
Manually annotated by BRENDA team
Bera, A.K.; Kuhn, R.J.; Smith, J.L.
Functional characterization of cis and trans activity of the Flavivirus NS2B-NS3 protease
J. Biol. Chem.
282
12883-12892
2007
Japanese encephalitis virus, West Nile virus, Yellow fever virus, Dengue virus type 2, Dengue virus type 4, West Nile virus NY99
Manually annotated by BRENDA team
Luo, D.; Vasudevan, S.G.; Lescar, J.
The flavivirus NS2B-NS3 protease-helicase as a target for antiviral drug development
Antiviral Res.
118
148-158
2015
Yellow fever virus (P03314), Murray Valley encephalitis virus (P05769), West Nile virus (P06935), Kunjin virus (P14335), dengue virus type I (P17763), Japanese encephalitis virus (P27395), Dengue virus type 2 (P29990), Dengue virus type 4 (Q2YHF0), Kokobera virus (Q32ZD5), Dengue virus type 3 (Q6YMS3), Dengue virus type 2 Thailand/16681/1984 (P29990), Dengue virus type 3 Martinique/1243/1999 (Q6YMS3), Yellow fever virus 17D vaccine (P03314), Dengue virus type 4 Thailand/0348/1991 (Q2YHF0), dengue virus type I Nauru/West Pac/1974 (P17763), Japanese encephalitis virus SA-14 (P27395), Kunjin virus MRM61C (P14335), Murray Valley encephalitis virus MVE-1-51 (P05769)
Manually annotated by BRENDA team