The Enzyme Database

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Accepted name: RNA helicase
Reaction: ATP + H2O = ADP + phosphate
Other name(s): 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
Systematic name: ATP phosphohydrolase (RNA helix unwinding)
Comments: RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. Some of them unwind RNA with a 3′ to 5′ polarity [3], other show 5′ to 3′ polarity [8]. Some helicases unwind DNA as well as RNA [7,8]. May be identical with EC (DNA helicase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Cordin, O., Tanner, N.K., Doere, M., Linder, P. and Banroques, J. The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity. EMBO J. 23 (2004) 2478–2487. [PMID: 15201868]
2.  Rodamilans, B. and Montoya, G. Expression, purification, crystallization and preliminary X-ray diffraction analysis of the DDX3 RNA helicase domain. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 (2007) 283–286. [PMID: 17401195]
3.  Lee, C.G. and Hurwitz, J. A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3′ to 5′ direction. J. Biol. Chem. 267 (1992) 4398–4407. [PMID: 1537828]
4.  Li, S.C., Chung, M.C. and Chen, C.S. Cloning and characterization of a DEAD box RNA helicase from the viable seedlings of aged mung bean. Plant Mol. Biol. 47 (2001) 761–770. [PMID: 11785937]
5.  Wu, J., Bera, A.K., Kuhn, R.J. and Smith, J.L. Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing. J. Virol. 79 (2005) 10268–10277. [PMID: 16051820]
6.  Gross, C.H. and Shuman, S. The nucleoside triphosphatase and helicase activities of vaccinia virus NPH-II are essential for virus replication. J. Virol. 72 (1998) 4729–4736. [PMID: 9573237]
7.  Frick, D.N. The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target. Curr. Issues Mol. Biol. 9 (2007) 1–20. [PMID: 17263143]
[EC created 2009]

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