BRENDA - Enzyme Database show
show all sequences of 1.3.98.3

Structural characterization reveals that viperin is a radical S-adenosyl-L-methionine (SAM) enzyme

Shaveta, G.; Shi, J.; Chow, V.T.; Song, J.; Biochem. Biophys. Res. Commun. 391, 1390-1395 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
viperin from monocytic cells, DNA and amino acid sequence determination and analysis, expression of His-tagged full-length enzyme, and of His-tagged viperin (45-361) and viperin (214-361) in Escherichia coli strain BL21
Homo sapiens
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
[4Fe-4S] cluster
Homo sapiens
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged full-length enzyme and viperin (214-361) from Escherichia coli strain BL21 inclusion bodies, solubilization by 8 M urea and purification by nickel affinity chromatography and gel filtration
Homo sapiens
Renatured (Commentary)
Commentary
Organism
recombinant soluble His-tagged viperin (45-361) from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant His-tagged full-length enzyme and viperin (214-361) from Escherichia coli strain BL21 inclusion bodies is solubilized by 8 M urea and further renaturated and purificated by nickel affinity chromatography and gel filtration. Reconstitution of the [4Fe-4S] cluster in Viperin residues 45-361, overview
Homo sapiens
Source Tissue
Source Tissue
Commentary
Organism
Textmining
monocyte
-
Homo sapiens
-
Subunits
Subunits
Commentary
Organism
More
structure analysis of recombinant His-tagged viperin (214-361) by UV-visible, circular dichroism, and NMR spectroscopy, overview
Homo sapiens
Cofactor
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Homo sapiens
[4Fe-4S]-center
-
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
viperin from monocytic cells, DNA and amino acid sequence determination and analysis, expression of His-tagged full-length enzyme, and of His-tagged viperin (45-361) and viperin (214-361) in Escherichia coli strain BL21
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Homo sapiens
[4Fe-4S]-center
-
Homo sapiens
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
[4Fe-4S] cluster
Homo sapiens
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged full-length enzyme and viperin (214-361) from Escherichia coli strain BL21 inclusion bodies, solubilization by 8 M urea and purification by nickel affinity chromatography and gel filtration
Homo sapiens
Renatured (Commentary) (protein specific)
Commentary
Organism
recombinant soluble His-tagged viperin (45-361) from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant His-tagged full-length enzyme and viperin (214-361) from Escherichia coli strain BL21 inclusion bodies is solubilized by 8 M urea and further renaturated and purificated by nickel affinity chromatography and gel filtration. Reconstitution of the [4Fe-4S] cluster in Viperin residues 45-361, overview
Homo sapiens
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
monocyte
-
Homo sapiens
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
structure analysis of recombinant His-tagged viperin (214-361) by UV-visible, circular dichroism, and NMR spectroscopy, overview
Homo sapiens
General Information
General Information
Commentary
Organism
physiological function
viperin is an interferon-inducible protein inhibiting a diverse spectrum of DNA and RNA viruses. It contains an N-terminal transmembrane helix, a highly conserved C-terminus and a middle region carrying a CX3CX2C motif, characteristic of radical S-adenosyl-L-methionine enzymes. The radical SAM enzyme activity may play a key role in the broad antiviral actions of viperin
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
physiological function
viperin is an interferon-inducible protein inhibiting a diverse spectrum of DNA and RNA viruses. It contains an N-terminal transmembrane helix, a highly conserved C-terminus and a middle region carrying a CX3CX2C motif, characteristic of radical S-adenosyl-L-methionine enzymes. The radical SAM enzyme activity may play a key role in the broad antiviral actions of viperin
Homo sapiens
Other publictions for EC 1.3.98.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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724235
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674567
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672473
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Structural and functional comp ...
Bacillus subtilis, Cupriavidus necator, Escherichia coli, Rhodobacter sphaeroides, Salmonella enterica subsp. enterica serovar Typhimurium
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655340
Layer
Crystal structure of coproporp ...
Escherichia coli
EMBO J.
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656073
Layer
Oxygen-independent coproporphy ...
Escherichia coli
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277
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