Dinoflagelat luciferaza
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| Dinoflagelat luciferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.13.12.18 | ||||||||
| CAS broj | 303183-71-3 | ||||||||
| 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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Dinoflagelat luciferaza (EC 1.13.12.18, (dinoflagellate luciferin) luciferaza, Gonyaulax luciferaza) je enzim sa sistematskim imenom dinoflagelat-luciferin:kiseonik 132-oksidoreduktaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Dinoflagellate luciferin + O2 oksidovani dinoflagellate luciferin + H2O + hnu
Luciferaza je prisutna dinoflagelatama kao što su Gonyaulax poliedra, Lingulodinium poliedrum, Noctiluca scintillans, i Pirocystis lunula. To je jednodelni protein sa tri luciferazna domena.
Reference[uredi | uredi kod]
- ↑ Dunlap, J.C. and Hastings, J.W. (1981). „The biological clock in Gonyaulax controls luciferase activity by regulating turnover”. J. Biol. Chem. 256: 10509-10518. PMID 7197271.
- ↑ Morse, D., Pappenheimer, A.M., Jr. and Hastings, J.W. (1989). „Role of a luciferin-binding protein in the circadian bioluminescent reaction of Gonyaulax polyedra”. J. Biol. Chem. 264: 11822-11826. PMID 2745419.
- ↑ Bae, Y.M. and Hastings, J.W. (1994). „Cloning, sequencing and expression of dinoflagellate luciferase DNA from a marine alga, Gonyaulax polyedra”. Biochim. Biophys. Acta 1219: 449-456. PMID 7918642.
- ↑ Li, L. (2000). „Gonyaulax luciferase: gene structure, protein expression, and purification from recombinant sources”. Methods Enzymol. 305: 249-258. PMID 10812605.
- ↑ Morse, D. and Mittag, M. (2000). „Dinoflagellate luciferin-binding protein”. Methods Enzymol. 305: 258-276. PMID 10812606.
- ↑ Schultz, L.W., Liu, L., Cegielski, M. and Hastings, J.W. (2005). „Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole”. Proc. Natl. Acad. Sci. USA 102: 1378-1383. PMID 15665092.
Literatura[uredi | uredi kod]
- 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.