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Literature summary for 2.7.7.84 extracted from

  • Tag-El-Din-Hassan, H.T.; Sasaki, N.; Torigoe, D.; Morimatsu, M.; Agui, T.
    Analysis of the relationship between enzymatic and antiviral activities of the chicken oligoadenylate synthetase-like (2017), J. Interferon Cytokine Res., 37, 71-80 .
    View publication on PubMed
Search for more literature for 2.7.7.84

Cloned(Commentary)

Cloned (Comment) Organism
gene OASL, wild-type and mutant enzymes are ectopically expressed in HEK 293FT cells to analyze the enzymatic activity, and in BHK-21 and BALB/3T3 cells to analyze the antiviral activity using WNV replicon Gallus gallus

Protein Variants

Protein Variants Comment Organism
additional information construction of enzyme mutants, ChOAS-L-A-FL, which is ChOAS-L-A conjugated with the Flag-Tag DYKDDDDK sequence, is used for generation of eight mutations: The DELTALxxxP domain, DELTAP-LooP domain, DELTAD-D box domain, 5 KR-RR-K193H (one AA substitution), DELTAKR-RR, and ChOAS-L-B (the other allele) are generated by site-directed mutagenesis. The other two mutations, DELTAUbL2 domain and DELTAUbL1/UbL2 domains, are generated in addition. All mutated variants are enzymatically inactive except for ChOAS-L-ADELTAUbL2, but all mutants shows antiviral activity to inhibit the replication of the WNV replicon except for the ChOAS-L-ADELTAUbL1/UbL2, which shows a partial inhibition compared to the wild-type ChOAS-L-A or the other mutant enzyme variants Gallus gallus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Gallus gallus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3 ATP Gallus gallus
-
 pppA2'p5'A2'p5'A + 2 diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Gallus gallus H9L0X6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3 ATP
-
 Gallus gallus pppA2'p5'A2'p5'A + 2 diphosphate
-
 ?

Synonyms

Synonyms Comment Organism
ChOAS-L
-
 Gallus gallus
OASL
-
 Gallus gallus
oligoadenylate synthetase-like
-
 Gallus gallus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Gallus gallus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Gallus gallus

General Information

General Information Comment Organism
physiological function enzyme ChOAS-L possesses enzymatic activity to convert ATP into 2'-5'-linked oligoadenylates and antiviral activity against West Nile virus (WNV) replicon, relationship between enzymatic and antiviral activities of the chicken oligoadenylate synthetase-like, overview. The ChOAS-L antiviral activity is independent of enzymatic activity. Analysis of the mechanism of antiviral activity against the flavivirus replication of ChOAS-L Gallus gallus