KEGG   ENZYME: 2.7.7.84Help
Entry
EC 2.7.7.84                 Enzyme                                 

Name
2'-5' oligoadenylate synthase;
OAS
Class
Transferases;
Transferring phosphorus-containing groups;
Nucleotidyltransferases
BRITE hierarchy
Sysname
ATP:ATP adenylyltransferase (2'-5' linkages-forming)
Reaction(IUBMB)
3 ATP = pppA2'p5'A2'p5'A + 2 diphosphate [RN:R10909]
Reaction(KEGG)
R10909;
(other) R10910
Show
Substrate
ATP [CPD:C00002]
Product
pppA2'p5'A2'p5'A [CPD:C20936];
diphosphate [CPD:C00013]
Comment
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].
History
EC 2.7.7.84 created 2013
Orthology
K14216  
2'-5'-oligoadenylate synthetase
Genes
HSA: 
4938(OAS1) 4939(OAS2) 4940(OAS3)
PTR: 
452267(OAS3) 739129(OAS1) 739230(OAS2)
PPS: 
100970211(OAS3) 100993699(OAS1) 103783986(OAS2)
GGO: 
101128307(OAS1) 101128904(OAS2) 101129249(OAS3)
PON: 
100172992(OAS1) 100443561(OAS3) 100444286(OAS2)
NLE: 
100587554(OAS1) 100587890(OAS3) 100588209(OAS2)
MCC: 
712265(OAS1) 712342(OAS3) 712401(OAS2)
MCF: 
102131636(OAS1) 102132016(OAS3) 102132392(OAS2)
RRO: 
CJC: 
100385368(OAS1) 100392459(OAS3) 103795420(OAS2)
MMU: 
23960(Oas1g) 23961(Oas1b) 246727(Oas3) 246728(Oas2) 246730(Oas1a)
RNO: 
192281(Oas1a) 246268(Oas1b) 363938(Oas2) 494202(Oas3)
CGE: 
NGI: 
HGL: 
101698818(Oas2) 101699903(Oas1)
OCU: 
100340530(OAS3) 100340787(OAS2)
TUP: 
102495865(OAS2) 106735200(OAS1)
CFA: 
477490(OAS3) 608778(OAS1) 611051(OAS2)
AML: 
100468112(OAS2) 100469118(OAS1) 100469368(OAS3)
UMR: 
103661196(OAS1) 103661197(OAS2) 103661290(OAS3)
FCA: 
101087875(OAS1) 101088116(OAS3) 102902426(OAS2)
PTG: 
102952232(OAS3) 107179395(OAS2)
BTA: 
347699(OAS1X) 529660(OAS2) 654488(OAS1Y)
BOM: 
PHD: 
102316296(OAS2) 102316872(OAS1)
CHX: 
OAS: 
SSC: 
397570(OAS1) 595128(OAS2)
CFR: 
102524147(OAS1)
BACU: 
LVE: 
103087433(OAS1) 103087703(OAS2)
ECB: 
100034147(OAS1) 791225(OAS3) 791250(OAS2)
MYB: 
MYD: 
102756142(OAS3) 102756409(OAS2) 102759968(OAS1)
PALE: 
102879074(OAS1) 102879322(OAS3) 102889470(OAS2)
MDO: 
100028774(OAS3) 100028903(OAS1)
SHR: 
AAM: 
106493520(OAS1)
ASN: 
AMJ: 
106737542(OAS1)
PSS: 
CMY: 
102937233(OAS3)
ACS: 
100562806(oas1)
PBI: 
GJA: 
LCM: 
CMK: 
BFO: 
SKO: 
LGI: 
CRG: 
NVE: 
 » show all
Taxonomy
Reference
1  [PMID:272640]
  Authors
Kerr IM, Brown RE
  Title
pppA2'p5'A2'p5'A: an inhibitor of protein synthesis synthesized with an enzyme fraction from interferon-treated cells.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 75 (1978) 256-60.
Reference
2  [PMID:456356]
  Authors
Martin EM, Birdsall NJ, Brown RE, Kerr IM
  Title
Enzymic synthesis, characterisation and nuclear-magnetic-resonance spectra of pppA2'p5'A2'p5'A and related oligonucleotides: comparison with chemically synthesised material.
  Journal
Eur. J. Biochem. 95 (1979) 295-307.
Reference
3  [PMID:14636576]
  Authors
Hartmann R, Justesen J, Sarkar SN, Sen GC, Yee VC
  Title
Crystal structure of the 2'-specific and double-stranded RNA-activated interferon-induced antiviral protein 2'-5'-oligoadenylate synthetase.
  Journal
Mol. Cell. 12 (2003) 1173-85.
  Sequence
[ssc:397570]
Reference
4  [PMID:17408844]
  Authors
Hovanessian AG, Justesen J
  Title
The human 2'-5'oligoadenylate synthetase family: unique interferon-inducible enzymes catalyzing 2'-5' instead of 3'-5' phosphodiester bond formation.
  Journal
Biochimie. 89 (2007) 779-88.
  Sequence
[hsa:4938 4939 4940]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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