DNK helikaza
DNK helikaza (EC 3.6.4.12, 3' to 5' DNK helikaza, 3'-5' DNK helikaza, 3'-5' PfDH, 5' to 3' DNK helikaza, AvDH1, BACH1 helikaza, BcMCM, BLM protein, BRCA1-asocirana C-terminalna helikaza, CeWRN-1, Dbp9p, DmRECQ5, DNK helikaza 120, DNK helikaza A, DNK helikaza E, DNK helikaza II, DNK helikaza III, DNK helikaza RECQL5beta, DNK helikaza VI, dnaB, DnaB helikaza E1, helikaza HDH IV, Hel E, helikaza DnaB, PcrA helikaza, UvrD, hHcsA, Hmi1p, hPif1, MCM helikaza, MCM protein, MER3 helikaza, MER3 protein, MPH1, PcrA, PcrA helikaza, PDH120, PfDH A, Pfh1p, PIF1) je enzim sa sistematskim imenom ATP fosfohidrolaza (odvijanje DNK heliksa).[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15] Ovaj enzim katalizuje sledeću hemijsku reakciju
DNK helikaza | |||||||||
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Identifikatori | |||||||||
EC broj | 3.6.4.12 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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DNK helikaze koriste energju ATP hidrolize za odvijanje dvolančanih DNK molekula.
Reference
uredi- ↑ Ozsoy, A.Z., Sekelsky, J.J. and Matson, S.W. (2001). „Biochemical characterization of the small isoform of Drosophila melanogaster RECQ5 helicase”. Nucleic Acids Res. 29: 2986-2993. PMID 11452023.
- ↑ 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. (2003). „The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5′ to 3′ viral helicases”. J. Biol. Chem. 278: 39578-39582. PMID 12917423.
- ↑ Nakagawa, T., Flores-Rozas, H. and Kolodner, R.D. (2001). „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: 31487-31493. PMID 11376001.
- ↑ Lee, C. and Seo, Y.S. (1998). „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: 377-386. PMID 9716495.
- ↑ Phan, T.N., Ehtesham, N.Z., Tuteja, R. and Tuteja, N. (2003). „A novel nuclear DNA helicase with high specific activity from Pisum sativum catalytically translocates in the 3′→5′ direction”. Eur. J. Biochem. 270: 1735-1745. PMID 12694186.
- ↑ Bernstein, D.A., Zittel, M.C. and Keck, J.L. (2003). „High-resolution structure of the E. coli RecQ helicase catalytic core”. EMBO J. 22: 4910-4921. PMID 14517231.
- ↑ Pike, A.C., Shrestha, B., Popuri, V., Burgess-Brown, N., Muzzolini, L., Costantini, S., Vindigni, A. and Gileadi, O. (2009). „Structure of the human RECQ1 helicase reveals a putative strand-separation pin”. Proc. Natl. Acad. Sci. USA 106: 1039-1044. PMID 19151156.
- ↑ Curti, E., Smerdon, S.J. and Davis, E.O. (2007). „Characterization of the helicase activity and substrate specificity of Mycobacterium tuberculosis UvrD”. J. Bacteriol. 189: 1542-1555. PMID 17158674.
- ↑ 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.
- ↑ 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. PMID 15220459.
- ↑ Ivessa, A.S., Zhou, J.Q., Schulz, V.P., Monson, E.K. and Zakian, V.A. (2002). „Saccharomyces Rrm3p, a 5′ to 3′ DNA helicase that promotes replication fork progression through telomeric and subtelomeric DNA”. Genes Dev. 16: 1383-1396. PMID 12050116.
- ↑ Zhou, J.Q., Qi, H., Schulz, V.P., Mateyak, M.K., Monson, E.K. and Zakian, V.A. (2002). „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: 2180-2191. PMID 12058079.
- ↑ George, T., Wen, Q., Griffiths, R., Ganesh, A., Meuth, M. and Sanders, C.M. (2009). „Human Pif1 helicase unwinds synthetic DNA structures resembling stalled DNA replication forks”. Nucleic Acids Res. 37: 6491-6502. PMID 19700773.
- ↑ Naqvi, A., Tinsley, E. and Khan, S.A. (2003). „Purification and characterization of the PcrA helicase of Bacillus anthracis”. J. Bacteriol. 185: 6633-6639. PMID 14594837.
- ↑ Ruiz-Maso, J.A., Anand, S.P., Espinosa, M., Khan, S.A. and del Solar, G. (2006). „Genetic and biochemical characterization of the Streptococcus pneumoniae PcrA helicase and its role in plasmid rolling circle replication”. J. Bacteriol. 188: 7416-7425. PMID 16936036.
Literatura
uredi- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.