Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | presence of a nucleoside triphosphate other than ATP also reduces the rate of 2'5' oligoadenylate formation indicating a competition between ATP and NTP for the donor site | Mus musculus | |
additional information | presence of a nucleoside triphosphate other than ATP also reduces the rate of 2'5'-oligoadenylate formation indicating a competition between ATP and NTP for the donor site | Oryctolagus cuniculus | |
NAD+ | - |
Gallus gallus | |
NAD+ | - |
Homo sapiens | |
NAD+ | - |
Mus musculus | |
NAD+ | - |
Oryctolagus cuniculus | |
tRNA | - |
Gallus gallus | |
tRNA | - |
Homo sapiens | |
tRNA | - |
Mus musculus | |
tRNA | - |
Oryctolagus cuniculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3 ATP | Gallus gallus | - |
pppA2'p5'A2'p5'A + 2 diphosphate | - |
? | |
3 ATP | Mus musculus | - |
pppA2'p5'A2'p5'A + 2 diphosphate | - |
? | |
3 ATP | Homo sapiens | - |
pppA2'p5'A2'p5'A + 2 diphosphate | - |
? | |
3 ATP | Oryctolagus cuniculus | - |
pppA2'p5'A2'p5'A + 2 diphosphate | - |
? | |
additional information | Oryctolagus cuniculus | the 2'5' oligoadenylate synthase has a multifunctional 2',5'-nucleotidyl-transferase activity | ? | - |
? | |
additional information | Gallus gallus | the 2'5' oligoadenylate synthetase has a multifunctional 2',5' nucleotidyl-transferase activity | ? | - |
? | |
additional information | Mus musculus | the 2'5' oligoadenylate synthetase has a multifunctional 2',5' nucleotidyl-transferase activity | ? | - |
? | |
additional information | Homo sapiens | the 2'5' oligoadenylate synthetase has a multifunctional 2',5' nucleotidyl-transferase activity | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Gallus gallus | - |
- |
- |
Homo sapiens | - |
- |
- |
Mus musculus | - |
- |
- |
Oryctolagus cuniculus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
cell culture | - |
Gallus gallus | - |
cell culture | from spleen | Homo sapiens | - |
L-929 cell | - |
Mus musculus | - |
reticulocyte | - |
Oryctolagus cuniculus | - |
spleen | - |
Homo sapiens | - |
WISH cell | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3 ATP | - |
Gallus gallus | pppA2'p5'A2'p5'A + 2 diphosphate | - |
? | |
3 ATP | - |
Mus musculus | pppA2'p5'A2'p5'A + 2 diphosphate | - |
? | |
3 ATP | - |
Homo sapiens | pppA2'p5'A2'p5'A + 2 diphosphate | - |
? | |
3 ATP | - |
Oryctolagus cuniculus | pppA2'p5'A2'p5'A + 2 diphosphate | - |
? | |
3 CTP | - |
Mus musculus | ? | - |
? | |
3 CTP | - |
Oryctolagus cuniculus | ? | - |
? | |
3 dATP | - |
Mus musculus | ? | - |
? | |
3 dATP | - |
Oryctolagus cuniculus | ? | - |
? | |
3 GTP | - |
Mus musculus | ? | - |
? | |
3 GTP | - |
Oryctolagus cuniculus | ? | - |
? | |
3 UTP | - |
Mus musculus | ? | - |
? | |
3 UTP | - |
Oryctolagus cuniculus | ? | - |
? | |
additional information | the 2'5' oligoadenylate synthase has a multifunctional 2',5'-nucleotidyl-transferase activity | Oryctolagus cuniculus | ? | - |
? | |
additional information | the 2'5' oligoadenylate synthetase has a multifunctional 2',5' nucleotidyl-transferase activity | Gallus gallus | ? | - |
? | |
additional information | the 2'5' oligoadenylate synthetase has a multifunctional 2',5' nucleotidyl-transferase activity | Mus musculus | ? | - |
? | |
additional information | the 2'5' oligoadenylate synthetase has a multifunctional 2',5' nucleotidyl-transferase activity | Homo sapiens | ? | - |
? | |
additional information | addition of high concentrations of tRNA (2 mg/ml) does not relieve the absolute dependence on double stranded RNA for 2' adenylation activity and 2'5' oligoadenylate synthetase activity in an extract of human Wish cells | Homo sapiens | ? | - |
? | |
additional information | besides accepting AMP, the NAD+ molecule can accept UMP, CMP, GMP and dAMP and probably other NMP catalyzed by the rabbit reticulocyte synthetase, UMP, CMP, and dAMP as well as AMP are incorporated into NAD+ at about half the rate of AMP incorporation into 2'5'-oligoadenylates, overview. A natural RNA, tRNA, can also be used as a primer for the 2' adenylation by both the the mouse L-cell enzyme. NADP+ does not serve as substrate | Mus musculus | ? | - |
? | |
additional information | besides accepting AMP, the NAD+ molecule can accept UMP, CMP, GMP, and dAMP and probably other NMP catalyzed by the rabbit reticulocyte synthetase, UMP, CMP, and dAMP as well as AMP are incorporated into NAD+ at about half the rate of AMP incorporation into 2'5' oligoadenylates, overview. A natural RNA, tRNA, can also be used as a primer for the 2' adenylation by both the rabbit reticulocyte enzyme. NADP+ does not serve as substrate | Oryctolagus cuniculus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
2'5' oligoadenylate synthetase | - |
Gallus gallus |
2'5' oligoadenylate synthetase | - |
Mus musculus |
2'5' oligoadenylate synthetase | - |
Homo sapiens |
2'5' oligoadenylate synthetase | - |
Oryctolagus cuniculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Oryctolagus cuniculus |
Organism | Comment | Expression |
---|---|---|
Gallus gallus | induction by interferon | up |
Mus musculus | induction by interferon | up |
Homo sapiens | induction by interferon | up |
Oryctolagus cuniculus | induction by interferon | up |
General Information | Comment | Organism |
---|---|---|
additional information | mechanism responsible for the inhibition of virus replication in interferon treated cells, overview | Mus musculus |
additional information | mechanism responsible for the inhibition of virus replication in interferon treated cells, overview | Homo sapiens |
physiological function | 2'5' oligoadenylate synthase catalyzes the synthesis of a series of 2'5' heteronucleotides with the general structure of pppA(pA)nPN and NAD-NMP. NAD+ acts as an acceptor for 2'-adenylation by the enzyme isolated from interferon treated chicken cell. The requirement for the acceptor site is an AMP group linked in a RpA configuration where R stands for pyrophosphate, NAD+, oligomeric or polymeric primers. NAD+ tRNA may play a regulatory role in 2'5'-oligoadenylates synthesis in the cell | Gallus gallus |
physiological function | 2'5' oligoadenylate synthase catalyzes the synthesis of a series of 2'5' heteronucleotides with the general structure of pppA(pA)nPN and NAD-NMP. The enzyme also catalyzes the 2' adenylation of tRNA. The requirement for the acceptor site is an AMP group linked in a RpA configuration where R stands for pyrophosphate, NAD+, oligomeric or polymeric primers. NAD+ tRNA may play a regulatory role in 2'5'-oligoadenylates synthesis in the cell | Mus musculus |
physiological function | 2'5' oligoadenylate synthase catalyzes the synthesis of a series of 2'5' heteronucleotides with the general structure of pppA(pA)nPN and NAD-NMP. The enzyme also catalyzes the 2' adenylation of tRNA. The requirement for the acceptor site is an AMP group linked in a RpA configuration where R stands for pyrophosphate, NAD+, oligomeric or polymeric primers. NAD+ tRNA may play a regulatory role in 2'5'-oligoadenylates synthesis in the cell | Homo sapiens |
physiological function | 2'5'-oligoadenylate synthase catalyzes the synthesis of a series of 2'5'-heteronucleotides with the general structure of pppA(pA)nPN and NAD-NMP. NAD+ acts as an acceptor for 2'-adenylation by the enzyme isolated from interferon treated chicken cell. The requirement for the acceptor site is an AMP group linked in a RpA configuration where R stands for pyrophosphate, NAD+, oligomeric or polymeric primers. NAD+ tRNA may play a regulatory role in 2'5'-oligoadenylates synthesis in the cell | Oryctolagus cuniculus |