Any feedback?
Information on EC 2.7.7.84 - 2'-5' oligoadenylate synthase and Organism(s) Sus scrofa and UniProt Accession Q29599
for references in articles please use BRENDA:EC2.7.7.84Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.7.84 2'-5' oligoadenylate synthaseIUBMB Comments
The enzyme is activated by binding to double-stranded RNA. The resulting product binds to and activates RNase L, which subsequently degrades the RNA. Oligoadenylates of chain lengths 2, 4 and 5 are also produced. The dimer does not have any known biological activity .
Specify your search results
Word Map
- 2.7.7.84
-
interferon-induced
-
ifn-induced
- ifn-alpha
- viruses
- interferon-alpha
-
ifn-beta
- ifn-gamma
- synthetases
- dsrna
-
ifn-stimulated
-
antiproliferative
- stomatitis
- interferon-beta
-
interferon-stimulated
-
myxovirus
- stat1
- alpha-interferon
-
interferon-treated
-
encephalomyocarditis
- neopterin
-
2-microglobulin
- flavivirus
-
daudi
-
ifn-treated
-
dsrna-dependent
-
2'-5'oligoadenylate
-
endoribonuclease
-
ifn-mediated
-
ifn-alpha-induced
- isg15
-
2-5a-dependent
-
dsrna-activated
- cydonium
-
ifn-dependent
-
polyi
-
rnasel
-
polyinosinic-polycytidylic
- geodia
-
interferon-mediated
-
ifn-resistant
-
anticellular
- analysis
- medicine
The taxonomic range for the selected organisms is: Sus scrofa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
2-5a synthetase, 2',5'-oligoadenylate synthetase, 2'-5'-oligoadenylate synthetase, 2'-5' oligoadenylate synthetase, oas1b, oas1a, 2'-5'-oligoadenylate synthetase 1, 2'-5'oas, 2'5' oligoadenylate synthetase, oligoadenylate synthetase-like, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
ATP:ATP adenylyltransferase (2'-5' linkages-forming)
The enzyme is activated by binding to double-stranded RNA. The resulting product binds to and activates RNase L, which subsequently degrades the RNA. Oligoadenylates of chain lengths 2, 4 and 5 are also produced. The dimer does not have any known biological activity [2].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dsRNA
2'-5'-oligoadenylate synthases are activated by viral double-stranded RNA in infected cells and initiate a cellular response by synthesizing 2'-5'-oligoadenylates, which in turn activate RNase L. All mammalian OAS proteins require dsRNA for activity ssRNA or DNA does not activate this class of enzymes. The dsRNA activator must be at least 15 nucleotides long, and no modification of the 2'-hydroxyl group is tolerated. OAS1 RNA activation site structure, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00044
ATP
wild-type OAS1, with ATP as sole substrate, pH and temperature not specified in the publication
0.0017
ATP
OAS1 mutant K212A, with ATP as sole substrate, pH and temperature not specified in the publication
0.0011
NAD+
OAS1 mutant S62A, with ATP and NAD+ as substrates, pH and temperature not specified in the publication
0.0013
NAD+
wild-type OAS1, with ATP and NAD+ as substrates, pH and temperature not specified in the publication
0.0014
NAD+
OAS1 mutant S63A, with ATP and NAD+ as substrates, pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.95
ATP
OAS1 mutant K212A, with ATP as sole substrate, pH and temperature not specified in the publication
8.1
ATP
wild-type OAS1, with ATP as sole substrate, pH and temperature not specified in the publication
0.99
NAD+
OAS1 mutant S62A, with ATP and NAD+ as substrates, pH and temperature not specified in the publication
3.6
NAD+
OAS1 mutant S63A, with ATP and NAD+ as substrates, pH and temperature not specified in the publication
3.6
NAD+
wild-type OAS1, with ATP and NAD+ as substrates, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0005
OAS1 mutant R38E/K41E/K59E/R194E/R198E, pH and temperature not specified in the publication
0.001
OAS1 mutant R194E/R198E, pH and temperature not specified in the publication
0.004
OAS1 mutant R198E, pH and temperature not specified in the publication
0.007
OAS1 mutant R198M, pH and temperature not specified in the publication
0.016
OAS1 mutant R38E/K41E, pH and temperature not specified in the publication
0.05
OAS1 mutant K203E, pH and temperature not specified in the publication
0.117
OAS1 mutant K59E, pH and temperature not specified in the publication
0.17
OAS1 mutant R194E, pH and temperature not specified in the publication
3.3
OAS1 mutant R245E/K246E, pH and temperature not specified in the publication
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
conserved catalytic mechanism for the 2'- and 3'-specific nucleotidyl transferases. specific nucleotidyl transferases. Comparison with structures of other superfamily members indicates that the donor substrates are bound by conserved active site features while the acceptor substrates are oriented by nonconserved regions
malfunction
mutation of the conserved Leu3 and Pro7 and of Cys330, Cys331, and Lys332 reduce enzyme activity. Mutants S62A and S63A display Michaelis-Menten kinetics toward NAD+, the kcat of the Ser62Ala mutant is approximately 3fold lower than the kcat for either the wild-type or the S63A mutant
physiological function
2'-5'-oligoadenylate synthases are interferon-induced, double-stranded RNA-activated antiviral enzymes which are the only proteins known to catalyze 2'-specific nucleotidyl transfer
additional information
additional information
-
OAS active site structure with three conserved active site aspartic acid residues, overview
additional information
OAS active site structure with three conserved active site aspartic acid residues, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). OAS1_PIG
349
0
40246
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
OAS1, purified recombinant porcine OAS1, 1.5 mg/ml protein in 50 mM NaCl, 10 mM HEPES, pH 6.8, 0.5 mM EDTA, with 5 mM of iodoacetamide for 30 min at room temperature, then concentrated to 6 mg/ml for crystallization by vapor diffusion, best crystals grow at 20°C in 1:1 drops with a well solution of 30% PEG 2000 MME, 0.2 M ammonium sulfate, and 0.1 M sodium cacodylate at pH 6, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K203E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K212A
the mutant has strongly impaired catalytic activity, KM for ATP is increased by almost 4fold relative to that of the wild-type protein, and kcat is decreased by roughly 8fold
K41E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K59E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R194E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R194E/R198E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R198E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R198M
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R245E/K246E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R38E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R38E/K41E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R38E/K41E/K59E/R194E/R198E
site-directed mutagenesis, the mutant is almost inactive
S62A
the mutant displays a strong substrate inhibition at higher ATP concentrations, more dramatic than that observed for wild-type OAS1
S63A
the mutant displays a strong substrate inhibition at higher ATP concentrations, more dramatic than that observed for wild-type OAS1
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant OAS1 from Escherichia coli strain BL21(DE3) by gel filtration, ammonium sulfate fractionation, heparin affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
OAS1, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
EXTERNAL LINKS (specific for EC-Number 2.7.7.84)
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
