Helikaza
Helikaze su klasa enzima koji su vitalni za sve žive organizme. One su motorni proteini koji se kreću duž fosfodiesterske osnove nukleinske kiseline, razdvajajući dva spojena lanca (i.e., DNK, RNK, ili RNK-DNK hibrid) koristeći energiju dobijenu iz ATP hidrolize.
| DNK helikaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
| RNK helikaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.6.4.13 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Funkcija
urediMnogi ćelijski procesi (replikacija DNK, transkripcija, translacija, rekombinacija, popravka DNK, ribozomska biogeneza) obuhvataju separaciju lanaca nukleinske kiseline. Helikaze se često koriste za razdvajanje lanaca DNK dvostrukog heliksa ili samostalno spojenih RNK molekula koristeći energiju ATP hidrolize. One se postepeno kreću duž jedne nukleinske kiseline dupleksa sa smerom i brzinom specifičnom za svaki pojedini enzim. Poznato je mnoštvo helikaza, i one proizvode znatnu raznovrsnost procesa u kojima je neophodna kataliza razdvajanja lanaca.[1][2][3]
Reference
uredi- ↑ Yuliang Wu, Kazuo Shin-ya and Robert M. Brosh Jr. (2008). „FANCJ Helicase Defective in Fanconia Anemia and Breast Cancer Unwinds G-Quadruplex DNA To Defend Genomic Stability”. Mol. Cell. Biol. 28 (12): 4116-4128. DOI:10.1128/MCB.02210-07. Arhivirano iz originala na datum 2013-05-06. Pristupljeno 2014-01-25.
- ↑ Haiyong Han, Richard J. Bennett, and Laurence H. Hurley (2000). „Inhibition of Unwinding of G-Quadruplex Structures by Sgs1 Helicase in the Presence of N,N‘-Bis[2-(1-piperidino)ethyl-3,4,9,10-perylenetetracarboxylic Diimide, a G-Quadruplex-Interactive Ligand”]. Biochemistry 39 (31): 9311–9316. DOI:10.1021/bi000482r.
- ↑ Haiyong Han, David R. Langley, Anupama Rangan, and Laurence H. Hurley (2001). „Selective Interactions of Cationic Porphyrins with G-Quadruplex Structures”. J. Am. Chem. Soc. 123 (37): 8902–8913. DOI:10.1021/ja002179j.
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.
Povezano
uredi- hromodomenske helikaze: CHD1, CHD1L, CHD2, CHD3, CHD4, CHD5, CHD6, CHD7, CHD8, CHD9
- DEAD kutija/DEAD/DEAH kutija helikaze: DDX3X, DDX5, DDX6, DDX10, DDX11, DDX12, DDX58, DHX8, DHX9, DHX37, DHX40, DHX58
- ASCC3, BLM, BRIP1, DNA2, FBXO18, FBXO30, HELB, HELLS, HELQ, HELZ, HFM1, HLTF, IFIH1, NAV2, PIF1, RECQL, RTEL1, SHPRH, SMARCA4, SMARCAL1, WRN, WRNIP1