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Literature summary for 2.1.1.56 extracted from

  • Ramadevi, N.; Burroughs, N.J.; Mertens, P.P.C.; Jones, I.M.
    Capping and methylation of mRNA by purified recombinant VP4 protein of bluetongue virus (1998), Proc. Natl. Acad. Sci. USA, 95, 13537-13542.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.56

Cloned(Commentary)

Cloned (Comment) Organism
expression of VP4 protein in Spodoptera frugiperda cells bluetongue virus

Protein Variants

Protein Variants Comment Organism
additional information mapping of lipid-binding site, membrane binding activity of wild-type and diverse constructed mutants bluetongue virus

General Stability

General Stability Organism
cardiolipin, phosphatidylglycerol, and phosphatidylserine bluetongue virus

Inhibitors

Inhibitors Comment Organism Structure
3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate i.e. CHAPS, strong inhibition bluetongue virus
deoxycholate inactivation bluetongue virus
Digitonin strong inhibition bluetongue virus
additional information detergents prevent the association of S-adenosyl-L-methionine with the enzyme bluetongue virus
N,N-bis-(3-D-gluconamidopropyl)-deoxycholamide strong inhibition bluetongue virus
n-octyl-beta-D-gluconpyranoside i.e. octylglucoside, strong inhibition bluetongue virus
N-tetradecyl-N,N-dimethyl-3-ammonio-1-propane sulfonate i.e. zwittergent 3-14, strong inhibition bluetongue virus
Thesit strong inhibition bluetongue virus
Triton X-100 inactivation, reversible by addition of lipids: cardiolipin, phosphatidylglycerol, and especially phosphatidylserine bluetongue virus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane lipid-binding site, membrane binding activity of wild-type and diverse mutants bluetongue virus 16020
-
viral nucleocapsid
-
 bluetongue virus 19013
-

Organism

Organism UniProt Comment Textmining
bluetongue virus
-
 enzyme activity belongs to VP4 protein
-

Purification (Commentary)

Purification (Comment) Organism
recombinant from Spodoptera frugiperda cells bluetongue virus

Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] RNA triphosphatase, RNA guanylyltransferase, and RNA (guanine-N7-)methyltransferase form the mRNA capping enzyme complex consiting of a small and a large subunit bluetongue virus
a
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] lipid-binding site, membrane binding activity of wild-type and diverse mutants bluetongue virus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + G(5')pppN N: G bluetongue virus S-adenosyl-L-homocysteine + m7G(5')pppG
-
 ?
S-adenosyl-L-methionine + G(5')pppN unmethylated cap analogue, serves as in vitro substrate bluetongue virus S-adenosyl-L-homocysteine + m7G(5')pppG
-
 ?
S-adenosyl-L-methionine + G(5')pppR-RNA
-
 bluetongue virus S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at bluetongue virus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at bluetongue virus