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)
CSAB: 103239154(OAS1) 103239155(OAS3) 103239156(OAS2)
RRO: 104666641(OAS1) 104666642(OAS3) 104666645
RBB: 108540456(OAS3) 108540457(OAS1) 108540462(OAS2)
CJC: 100385368(OAS1) 100392459(OAS3) 103795420(OAS2)
SBQ: 101043239(OAS2) 101043563(OAS3) 101043879(OAS1)
MMU: 23960(Oas1g) 23961(Oas1b) 246727(Oas3) 246728(Oas2) 246730(Oas1a)
RNO: 192281(Oas1a) 246268(Oas1b) 363938(Oas2) 494202(Oas3)
HGL: 101698818(Oas2) 101699903(Oas1)
OCU: 100340530(OAS3) 100340787(OAS2) 108178670(OAS1)
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)
ORO: 101369458(OAS2) 101373749(OAS1) 101374040(OAS3)
FCA: 101087875(OAS1) 101088116(OAS3) 102902426(OAS2)
PTG: 102952232(OAS3) 107179395(OAS2)
AJU: 106982083
BTA: 347699(OAS1X) 519922(OAS1Z) 529660(OAS2) 654488(OAS1Y)
PHD: 102316296(OAS2) 102316872(OAS1)
SSC: 397570(OAS1) 595128(OAS2)
CFR: 102524147(OAS1)
LVE: 103087433(OAS1) 103087703(OAS2)
OOR: 101277868(OAS2) 101289192
ECB: 100034147(OAS1) 791225(OAS3) 791250(OAS2)
EAI: 106842212 106842249(OAS1)
MYB: 102247108(OAS1) 102251057(OAS2) 102258838
MYD: 102756142(OAS3) 102756409(OAS2) 102759968(OAS1)
RSS: 109448590(OAS3) 109448591(OAS2) 109448614(OAS1)
PALE: 102879074(OAS1) 102879322(OAS3) 102889470(OAS2)
LAV: 100659469(OAS2) 104846792(OAS3) 104846793(OAS1)
MDO: 100028774(OAS3) 100028903(OAS1)
AAM: 106493520(OAS1)
ASN: 102383736
AMJ: 106737542(OAS1)
CMY: 102937233(OAS3)
CPIC: 101945210
ACS: 100562806(oas1)
PBI: 103053194
LCM: 102355743
CMK: 103184093
SKO: 102802564
AQU: 105316703
 » 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 75:256-60 (1978)
DOI:10.1073/pnas.75.1.256
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 95:295-307 (1979)
DOI:10.1111/j.1432-1033.1979.tb12965.x
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 12:1173-85 (2003)
DOI:10.1016/S1097-2765(03)00433-7
  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 89:779-88 (2007)
DOI:10.1016/j.biochi.2007.02.003
  Sequence
[hsa:4938 4939 4940]
Other DBs
ExplorEnz - The Enzyme Database: 2.7.7.84
IUBMB Enzyme Nomenclature: 2.7.7.84
ExPASy - ENZYME nomenclature database: 2.7.7.84
BRENDA, the Enzyme Database: 2.7.7.84

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