Any feedback?
Literature summary for 2.7.7.84 extracted from
- In silico identification of potential inhibitors against human 2'-5'-oligoadenylate synthetase (OAS) proteins (2020), Comput. Biol. Chem., 85, 107211 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene OAS1, sequence comparisons | Homo sapiens |
| gene OAS2, sequence comparisons | Homo sapiens |
| gene OAS3, sequence comparisons | Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| OAS crystal structures analysis | Homo sapiens |
| OAS crystal structures analysis, PDB ID 4IG8 | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | inhibitor screening and identification of 12 compounds exerting competitive inhibition in the ATP binding site1 of OAS1 protein, independently of the activation state of the enzyme, docking and interaction study. Although there is little correlation between specific chemical fragments and their interactions, intermolecular contacts with OAS catalytic triad and other critical amino acids are mainly promoted by heterocycles with Pi electrons and hydrogen bond acceptors; inhibitor screening and identification of 18 compounds exerting competitive inhibition in the ATP binding site of OAS2 protein, independently of the activation state of the enzyme, docking and interaction study. Although there is little correlation between specific chemical fragments and their interactions, intermolecular contacts with OAS catalytic triad and other critical amino acids are mainly promoted by heterocycles with Pi electrons and hydrogen bond acceptors; inhibitor screening and identification of 7 compounds exerting competitive inhibition in the ATP binding site of OAS3 protein, independently of the activation state of the enzyme, docking and interaction study. Although there is little correlation between specific chemical fragments and their interactions, intermolecular contacts with OAS catalytic triad and other critical amino acids are mainly promoted by heterocycles with Pi electrons and hydrogen bond acceptors | Homo sapiens | |
| ZINC06786354 | - |
Homo sapiens | |
| ZINC06900324 | - |
Homo sapiens | |
| ZINC09561278 | - |
Homo sapiens | |
| ZINC09561285 | - |
Homo sapiens | |
| ZINC09561289 | - |
Homo sapiens | |
| ZINC09561296 | - |
Homo sapiens | |
| ZINC20417720 | - |
Homo sapiens | |
| ZINC33034925 | - |
Homo sapiens |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | activates, after stimulation with dsRNA, OAS requires two Mg2+ ions and two molecules of ATP to perform its enzymatic activity. The Mg2+ ions play a critical role in positioning the substrates in an ideal geometry for the reaction, binding structure modeling, overview | Homo sapiens |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3 ATP | Homo sapiens | - |
pppA2'p5'A2'p5'A + 2 diphosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P00973 | - |
- |
| Homo sapiens | P29728 | - |
- |
| Homo sapiens | Q9Y6K5 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3 ATP | - |
Homo sapiens | pppA2'p5'A2'p5'A + 2 diphosphate | - |
? | |
| 3 ATP | during the synthesis of 2-5A, one ATP, known as the donor, transfers its AMP moiety to a second ATP, known as the acceptor. For polymerization, the acceptor ATP is replaced by a growing chain of 2-5A | Homo sapiens | pppA2'p5'A2'p5'A + 2 diphosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 2'-5'-oligoadenylate synthetase | - |
Homo sapiens |
| OAS | - |
Homo sapiens |
| OAS1 | - |
Homo sapiens |
| OAS2 | - |
Homo sapiens |
| OAS3 | - |
Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | activates, after stimulation with dsRNA, OAS requires two Mg2+ ions and two molecules of ATP to perform its enzymatic activity. Residues Ser396, Gln528, Lys547, Lys566, and Tyr567 are involved in positioning of the donor ATP, while residues Val412, Arg463, Leu483, Ser 521, Thr522, Thr525, and Gln528 are involved in positioning of the acceptor ATP | Homo sapiens | |
| ATP | activates, after stimulation with dsRNA, OAS requires two Mg2+ ions and two molecules of ATP to perform its enzymatic activity. Residues Ser63, Gln194, Lys213, Gln229, and Tyr230 are involved in positioning of the donor ATP, while residues Val79, Arg130, Leu150, Ser 187, Thr188, Thr191, and Gln194 are involved in positioning of the acceptor ATP | Homo sapiens | |
| ATP | activates, after stimulation with dsRNA, OAS requires two Mg2+ ions and two molecules of ATP to perform its enzymatic activity. Residues Ser804, Gln931, Lys950, Gln969, and His970 are involved in positioning of the donor ATP, while residues Val820, Arg869, Leu890, Ser924, Thr925, Thr928, and Gln931 are involved in positioning of the acceptor ATP | Homo sapiens | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | enzyme structure homology modeling. The active site is formed by residues Asp408, Asp410, Asp481 | Homo sapiens |
| additional information | enzyme structure homology modeling. The active site is formed by residues Asp75, Asp77, Asp148 | Homo sapiens |
| additional information | enzyme structure homology modeling. The active site is formed by residues Asp816, Asp818, Asp888 | Homo sapiens |
| physiological function | as part of the type I IFN signaling, the 2'-5'-oligoadenylate synthetase (OAS) proteins are involved in the progression of several non-viral diseases. OAS is correlated with immune-modulatory functions that promote chronic inflammatory conditions, autoimmune disorders, cancer, and infectious diseases | Homo sapiens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
