Retroviralna ribonukleaza H
(Preusmjereno sa stranice RT/RNaza H)
Retroviralna ribonukleaza H (EC 3.1.26.13, RT/RNaza H, retroviralna reverzna transkriptaza RNazaH, HIV RNaza H) je enzim.[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Retroviralna ribonukleaza H | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.1.26.13 | ||||||||
| CAS broj | 9050-76-4 | ||||||||
| 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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- Endohidroliza RNK u RNK/DNK hibride. Postoje tri različita moda razlaganja
- za sekvencu-specifično unutrašnje razlaganje RNK. Enzimi HIV tip 1 i Moloni murin leukemija virusa preferentno razlažu RNK na mestu jedan nukleotid udaljenom od RNK-DNK spoja.
- Prema RNK 5'-kraju usmereno odvajanje 13-19 nukleotida sa RNK kraja.
- Prema DNK 3'-kraju usmereno odvajanje 15-20 nukleotida sa prajmer kraja.
Retroviralna reverzna transkriptaza je multifunkcionalni enzim odgovoran za viralnu replikaciju.
Reference uredi
- ↑ Schultz, S.J., Zhang, M. and Champoux, J.J. (2004). „Recognition of internal cleavage sites by retroviral RNases H”. J. Mol. Biol. 344: 635-652. PMID 15533434.
- ↑ Sarafianos, S.G., Das, K., Tantillo, C., Clark, A.D., Jr., Ding, J., Whitcomb, J.M., Boyer, P.L., Hughes, S.H. and Arnold, E. (2001). „Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNA”. EMBO J. 20: 1449-1461. PMID 11250910.
- ↑ Rausch, J.W., Lener, D., Miller, J.T., Julias, J.G., Hughes, S.H. and Le Grice, S.F. (2002). „Altering the RNase H primer grip of human immunodeficiency virus reverse transcriptase modifies cleavage specificity”. Biochemistry 41: 4856-4865. PMID 11939780.
- ↑ Brehm, J.H., Mellors, J.W. and Sluis-Cremer, N. (2008). „Mechanism by which a glutamine to leucine substitution at residue 509 in the ribonuclease H domain of HIV-1 reverse transcriptase confers zidovudine resistance”. Biochemistry 47: 14020-14027. PMID 19067547.
- ↑ Schultz, S.J., Zhang, M., Kelleher, C.D. and Champoux, J.J. (2000). „Analysis of plus-strand primer selection, removal, and reutilization by retroviral reverse transcriptases”. J. Biol. Chem. 275: 32299-32309. PMID 10913435.
- ↑ DeStefano, J.J., Mallaber, L.M., Fay, P.J. and Bambara, R.A. (1993). „Determinants of the RNase H cleavage specificity of human immunodeficiency virus reverse transcriptase”. Nucleic Acids Res. 21: 4330-4338. PMID 7692401.
- ↑ Kati, W.M., Johnson, K.A., Jerva, L.F. and Anderson, K.S. (1992). „Mechanism and fidelity of HIV reverse transcriptase”. J. Biol. Chem. 267: 25988-25997. PMID 1281479.
- ↑ Palaniappan, C., Fuentes, G.M., Rodriguez-Rodriguez, L., Fay, P.J. and Bambara, R.A. (1996). „Helix structure and ends of RNA/DNA hybrids direct the cleavage specificity of HIV-1 reverse transcriptase RNase H”. J. Biol. Chem. 271: 2063-2070. PMID 8567660.
- ↑ Fu, T.B. and Taylor, J. (1992). „When retroviral reverse transcriptases reach the end of their RNA templates”. J. Virol. 66: 4271-4278. PMID 1376369.
- ↑ Beilhartz, G.L., Wendeler, M., Baichoo, N., Rausch, J., Le Grice, S. and Gotte, M. (2009). „HIV-1 reverse transcriptase can simultaneously engage its DNA/RNA substrate at both DNA polymerase and RNase H active sites: implications for RNase H inhibition”. J. Mol. Biol. 388: 462-474. PMID 19289131.
- ↑ Huang, H., Chopra, R., Verdine, G.L. and Harrison, S.C. (1998). „Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance”. Science 282: 1669-1675. PMID 9831551.
- ↑ Krug, M.S. and Berger, S.L. (1989). „Ribonuclease H activities associated with viral reverse transcriptases are endonucleases”. Proc. Natl. Acad. Sci. USA 86: 3539-3543. PMID 2471188.
- ↑ Champoux, J.J. and Schultz, S.J. (2009). „Ribonuclease H: properties, substrate specificity and roles in retroviral reverse transcription”. FEBS J. 276: 1506-1516. PMID 19228195.
- ↑ Schultz, S.J. and Champoux, J.J. (2008). „RNase H activity: structure, specificity, and function in reverse transcription”. Virus Res. 134: 86-103. PMID 18261820.
- ↑ Goedken, E.R. and Marqusee, S. (1999). „Metal binding and activation of the ribonuclease H domain from moloney murine leukemia virus”. Protein Eng. 12: 975-980. PMID 10585503.
- ↑ Davies, J.F., 2nd, Hostomska, Z., Hostomsky, Z., Jordan, S.R. and Matthews, D.A. (1991). „Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase”. Science 252: 88-95. PMID 1707186.
- ↑ Pari, K., Mueller, G.A., DeRose, E.F., Kirby, T.W. and London, R.E. (2003). „Solution structure of the RNase H domain of the HIV-1 reverse transcriptase in the presence of magnesium”. Biochemistry 42: 639-650. PMID 12534276.
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.