The Enzyme Database

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Accepted name: DNA helicase
Reaction: ATP + H2O = ADP + phosphate
Other name(s): 3′ to 5′ DNA helicase; 3′-5′ DNA helicase; 3′-5′ PfDH; 5′ to 3′ DNA helicase; AvDH1; BACH1 helicase; BcMCM; BLM protein; BRCA1-associated C-terminal helicase; CeWRN-1; Dbp9p; DmRECQ5; DNA helicase 120; DNA helicase A; DNA helicase E; DNA helicase II; DNA helicase III; DNA helicase RECQL5β; DNA helicase VI; dnaB; DnaB helicase E1; helicase HDH IV; Hel E; helicase DnaB; helicase domain of bacteriophage T7 gene 4 protein helicase; PcrA helicase; UvrD; hHcsA; Hmi1p; hPif1; MCM helicase; MCM protein; MER3 helicase; MER3 protein; MPH1; PcrA; PcrA helicase; PDH120; PfDH A; Pfh1p; PIF1
Systematic name: ATP phosphohydrolase (DNA helix unwinding)
Comments: DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. Some of them unwind duplex DNA with a 3′ to 5′ polarity [1,3,5,8], others show 5′ to 3′ polarity [10,11,12,13] or unwind DNA in both directions [14,15]. Some helicases unwind DNA as well as RNA [9,10]. May be identical with EC (RNA helicase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Ozsoy, A.Z., Sekelsky, J.J. and Matson, S.W. Biochemical characterization of the small isoform of Drosophila melanogaster RECQ5 helicase. Nucleic Acids Res. 29 (2001) 2986–2993. [DOI] [PMID: 11452023]
2.  Tanner, J.A., Watt, R.M., Chai, Y.B., Lu, L.Y., Lin, M.C., Peiris, J.S., Poon, L.L., Kung, H.F. and Huang, J.D. The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5′ to 3′ viral helicases. J. Biol. Chem. 278 (2003) 39578–39582. [DOI] [PMID: 12917423]
3.  Nakagawa, T., Flores-Rozas, H. and Kolodner, R.D. The MER3 helicase involved in meiotic crossing over is stimulated by single-stranded DNA-binding proteins and unwinds DNA in the 3′ to 5′ direction. J. Biol. Chem. 276 (2001) 31487–31493. [DOI] [PMID: 11376001]
4.  Lee, C. and Seo, Y.S. Isolation and characterization of a processive DNA helicase from the fission yeast Schizosaccharomyces pombe that translocates in a 5′-to-3′ direction. Biochem. J. 334 (1998) 377–386. [PMID: 9716495]
5.  Phan, T.N., Ehtesham, N.Z., Tuteja, R. and Tuteja, N. A novel nuclear DNA helicase with high specific activity from Pisum sativum catalytically translocates in the 3′→5′ direction. Eur. J. Biochem. 270 (2003) 1735–1745. [DOI] [PMID: 12694186]
6.  Bernstein, D.A., Zittel, M.C. and Keck, J.L. High-resolution structure of the E. coli RecQ helicase catalytic core. EMBO J. 22 (2003) 4910–4921. [DOI] [PMID: 14517231]
7.  Pike, A.C., Shrestha, B., Popuri, V., Burgess-Brown, N., Muzzolini, L., Costantini, S., Vindigni, A. and Gileadi, O. Structure of the human RECQ1 helicase reveals a putative strand-separation pin. Proc. Natl. Acad. Sci. USA 106 (2009) 1039–1044. [DOI] [PMID: 19151156]
8.  Curti, E., Smerdon, S.J. and Davis, E.O. Characterization of the helicase activity and substrate specificity of Mycobacterium tuberculosis UvrD. J. Bacteriol. 189 (2007) 1542–1555. [DOI] [PMID: 17158674]
9.  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]
10.  Ivanov, K.A. and Ziebuhr, J. Human coronavirus 229E nonstructural protein 13: characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5′-triphosphatase activities. J. Virol. 78 (2004) 7833–7838. [DOI] [PMID: 15220459]
11.  Ivessa, A.S., Zhou, J.Q., Schulz, V.P., Monson, E.K. and Zakian, V.A. Saccharomyces Rrm3p, a 5′ to 3′ DNA helicase that promotes replication fork progression through telomeric and subtelomeric DNA. Genes Dev. 16 (2002) 1383–1396. [DOI] [PMID: 12050116]
12.  Zhou, J.Q., Qi, H., Schulz, V.P., Mateyak, M.K., Monson, E.K. and Zakian, V.A. Schizosaccharomyces pombe pfh1+ encodes an essential 5′ to 3′ DNA helicase that is a member of the PIF1 subfamily of DNA helicases. Mol. Biol. Cell 13 (2002) 2180–2191. [PMID: 12058079]
13.  George, T., Wen, Q., Griffiths, R., Ganesh, A., Meuth, M. and Sanders, C.M. Human Pif1 helicase unwinds synthetic DNA structures resembling stalled DNA replication forks. Nucleic Acids Res. 37 (2009) 6491–6502. [DOI] [PMID: 19700773]
14.  Naqvi, A., Tinsley, E. and Khan, S.A. Purification and characterization of the PcrA helicase of Bacillus anthracis. J. Bacteriol. 185 (2003) 6633–6639. [DOI] [PMID: 14594837]
15.  Ruiz-Maso, J.A., Anand, S.P., Espinosa, M., Khan, S.A. and del Solar, G. Genetic and biochemical characterization of the Streptococcus pneumoniae PcrA helicase and its role in plasmid rolling circle replication. J. Bacteriol. 188 (2006) 7416–7425. [DOI] [PMID: 16936036]
[EC created 2009]

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