RNA helicase

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RNA helicase
Identifiers
EC number 3.6.4.13
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

RNA helicase (EC 3.6.4.13, CSFV NS3 helicase, DBP2, DbpA, DDX17, DDX25, DDX3, DDX3X, DDX3Y, DDX4, DDX5, DEAD-box protein DED1, DEAD-box RNA helicase, DEAH-box protein 2, DEAH-box RNA helicase, DED1, Dex(H/D) RNA helicase, EhDEAD1, EhDEAD1 RNA helicase, eIF4A helicase, KOKV helicase, Mtr4p, nonstructural protein 3 helicase, NPH-II, RHA, RNA helicase A, RNA helicase DDX3, RNA helicase Hera, RNA-dependent ATPase, TGBp1 NTPase/helicase domain, VRH1, GRTH/DDX25) is an enzyme with system name ATP phosphohydrolase (RNA helix unwinding).[1][2][3][4][5][6][7][8] This enzyme catalyses the following chemical reaction

ATP + H2O \rightleftharpoons ADP + phosphate

RNA helicases utilize the energy from ATP hydrolysis to unwind RNA.

References[edit]

  1. ^ Cordin, O., Tanner, N.K., Doere, M., Linder, P. and Banroques, J. (2004). "The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity". EMBO J. 23: 2478–2487. doi:10.1038/sj.emboj.7600272. PMID 15201868. 
  2. ^ Rodamilans, B. and Montoya, G. (2007). "Expression, purification, crystallization and preliminary X-ray diffraction analysis of the DDX3 RNA helicase domain". Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63: 283–286. doi:10.1107/s1744309107006434. PMID 17401195. 
  3. ^ Lee, C.G. and Hurwitz, J. (1992). "A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3′ to 5′ direction". J. Biol. Chem. 267: 4398–4407. PMID 1537828. 
  4. ^ Li, S.C., Chung, M.C. and Chen, C.S. (2001). "Cloning and characterization of a DEAD box RNA helicase from the viable seedlings of aged mung bean". Plant Mol. Biol. 47: 761–770. PMID 11785937. 
  5. ^ Wu, J., Bera, A.K., Kuhn, R.J. and Smith, J.L. (2005). "Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing". J. Virol. 79: 10268–10277. doi:10.1128/jvi.79.16.10268-10277.2005. PMID 16051820. 
  6. ^ Gross, C.H. and Shuman, S. (1998). "The nucleoside triphosphatase and helicase activities of vaccinia virus NPH-II are essential for virus replication". J. Virol. 72: 4729–4736. PMID 9573237. 
  7. ^ Frick, D.N. (2007). "The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target". Curr. Issues Mol. Biol. 9: 1–20. PMID 17263143. 
  8. ^ Ivanov, K.A. and Ziebuhr, J. (2004). "Human coronavirus 229E nonstructural protein 13: characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5′-triphosphatase activities". J. Virol. 78: 7833–7838. doi:10.1128/jvi.78.14.7833-7838.2004. PMID 15220459. 

See also[edit]

External links[edit]