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Literature summary for 2.7.7.84 extracted from

  • Ferbus, D.; Justesen, J.; Besancon, F.; Thang, M.
    The 2'5' oligoadenylate synthetase has a multifunctional 2',5' nucleotidyl-transferase activity (1981), Biochem. Biophys. Res. Commun., 100, 847-856.
    View publication on PubMed

Inhibitors

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/ 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
-
?
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

Organism UniProt Comment Textmining
Gallus gallus
-
-
-
Homo sapiens
-
-
-
Mus musculus
-
-
-
Oryctolagus cuniculus
-
-
-

Source Tissue

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 and Products (Substrate)

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Oryctolagus cuniculus

Expression

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

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