Dinoflagellate luciferase (EC 1.13.12.18, Gonyaulax luciferase) is a specific luciferase, an enzyme with systematic name dinoflagellate-luciferin:oxygen 132-oxidoreductase.[1][2][3][4][5] [6]
| Dinoflagellate luciferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.13.12.18 | ||||||||
| CAS no. | 303183-71-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- dinoflagellate luciferin + O2 oxidized dinoflagellate luciferin + H2O + hnu
Mechanism of Reaction
editThe EC number of dinoflagellate luciferase is 1.13.12.18. This number denotes that dinoflagellate luciferase is an oxidoreductase that acts on single donors with incorporation of molecular oxygen (oxygenases) that are not necessarily derived from O2, with incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases).[7]
Structure
editDinoflagellate luciferase is a single protein with three luciferase domains and an N-terminal domain.[6] The three domains have been shown to be 1.8-A crystal structure that contain beta barrel pocketa that act as active sites with each domain preceded by a regulatory three helix bundle.[6] These helical bundles contain important histidine residues that play a role in the pH regulation of dinoflagellate luciferase activity.[6] Specifically, the presence of N-terminal intramolecularly conserved histidine residues are shown to be responsible for the loss of activity of the enzyme at high pH.[8] Protonation of these histidine residues alters the conformation of each domain to allow the substrate luciferin to enter the enlarged pocket. This conformational change must occur in order to provide access and space for the ligand to enter the active site.[6] At pH 8, the histidine residues remain unprotonated, interacting with a network of hydrogen bonds that block substrate access to the active site.[6] This blockage is overcome by protonation of histidine residues or by experimental replacement of histidine residues with alanine residues.[6] Realistically, alanine replacement does not occur spontaneously; however, this experimental result provides further evidence that the larger histidine residues block access to the active site of the enzyme. The N-terminal domain is conserved between dinoflagellate luciferase and luciferin binding proteins. This region may be where luciferin binding proteins interact with luciferase in order to allow the ligand, usually luciferin, to enter the active site.[9]
Reaction Conditions
editDinoflagellate luciferase is active in slightly acidic environments but in most cases requires the luciferin binding protein (LBP) to unbind from the dinoflagellate luciferin substrate; however, LBP binds luciferin at neutral to alkaline conditions.[10] Although the primary mechanism is unknown, voltage-gated ion channels on scintillon membranes open, allowing an influx of protons to enter the organelle lowering the pH sufficiently for dinoflagellate luciferase to activate.[11] G-protein coupled receptors and calcium ions also play a role in stimulating bioluminescence.[12]
Applications
editDinoflagellate luciferase is found in bioluminescent dinoflagellates, eukaryotic protists that are found in ocean surface waters.[13] Dinoflagellate luciferase allows these organisms to emit blue light (max 475 nm) after stimulation.[14] The light produced is theorized to act as a defense against predators or lure for prey.[15] These organisms utilize scintillons which are specialized organelles that project from the cytoplasm into the acidic vacuole to produce this light.[16] This is where the dinoflagellate luciferase enzyme is contained.
References
edit- ^ Dunlap JC, Hastings JW (October 1981). "The biological clock in Gonyaulax controls luciferase activity by regulating turnover". The Journal of Biological Chemistry. 256 (20): 10509–18. doi:10.1016/S0021-9258(19)68651-5. PMID 7197271.
- ^ Morse D, Pappenheimer AM, Hastings JW (July 1989). "Role of a luciferin-binding protein in the circadian bioluminescent reaction of Gonyaulax polyedra". The Journal of Biological Chemistry. 264 (20): 11822–6. doi:10.1016/S0021-9258(18)80139-9. PMID 2745419.
- ^ Bae YM, Hastings JW (October 1994). "Cloning, sequencing and expression of dinoflagellate luciferase DNA from a marine alga, Gonyaulax polyedra". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1219 (2): 449–56. doi:10.1016/0167-4781(94)90071-x. PMID 7918642.
- ^ Li L (2000). "Gonyaulax luciferase: gene structure, protein expression, and purification from recombinant sources". Bioluminescence and Chemiluminescence Part C. Methods in Enzymology. Vol. 305. pp. 249–58. doi:10.1016/s0076-6879(00)05492-6. ISBN 9780121822064. PMID 10812605.
- ^ Morse D, Mittag M (2000). "Dinoflagellate luciferin-binding protein". Bioluminescence and Chemiluminescence Part C. Methods in Enzymology. Vol. 305. pp. 258–76. doi:10.1016/s0076-6879(00)05493-8. ISBN 9780121822064. PMID 10812606.
- ^ a b c d e f g Schultz LW, Liu L, Cegielski M, Hastings JW (February 2005). "Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole". Proceedings of the National Academy of Sciences of the United States of America. 102 (5): 1378–83. Bibcode:2005PNAS..102.1378S. doi:10.1073/pnas.0409335102. PMC 547824. PMID 15665092.
- ^ Embl-Ebi. (n.d.). Intenz. Intenz - Rules on enzyme classification. Retrieved October 9, 2021, from https://www.ebi.ac.uk/intenz/rules.jsp#scheme1.
- ^ Li, L., Liu, L., Hong, R., Robertson, D., & Hastings, J. W. (2001). N-terminal intramolecularly conserved histidine residues of three domains in Gonyaulax luciferase are responsible for loss of activity in the alkaline region. Biochemistry, 40(6), 1844–1849. https://doi.org/10.1021/bi002094v
- ^ Okamoto OK, Liu L, Robertson DL, Hastings JW (Dec 2001). "Members of a dinoflagellate luciferase gene family differ in synonymous substitution rates". Biochemistry. 40 (51): 15862–68. CiteSeerX 10.1.1.494.3563. doi:10.1021/bi011651q. PMID 11747464.
- ^ Fogel M, Schmitter RE, Hastings JW. On the physical identity of scintillons: bioluminescent particles in Gonyaulax polyedra. J Cell Sci. 1972 Jul;11(1):305-17. PMID 4341991.
- ^ Chen, A. K., Latz, M. I., Sobolewski, P., & Frangos, J. A. (2007). Evidence for the role of G-proteins in flow stimulation of dinoflagellate bioluminescence. American journal of physiology. Regulatory, integrative and comparative physiology, 292(5), R2020–R2027. https://doi.org/10.1152/ajpregu.00649.2006
- ^ von Dassow, P., & Latz, M. I. (2002). The role of Ca(2+) in stimulated bioluminescence of the dinoflagellate Lingulodinium polyedrum. The Journal of experimental biology, 205(Pt 19), 2971–2986.
- ^ Tett, P. (1971). The Relation between Dinoflagellates and the Bioluminescence of Sea Water. Journal of the Marine Biological Association of the United Kingdom, 51(1), 183-206. doi:10.1017/S002531540000655X
- ^ Nakamura, H., Kishi, Y., Shimomura, O., Morse, D., & Hastings, J. W. (1989). Structure of dinoflagellate luciferin and its enzymic and nonenzymic air-oxidation products. Journal of the American Chemical Society, 111(19), 7607–7611. https://doi.org/10.1021/ja00201a050
- ^ Marcinko, C. L. J., Painter, S. C., Martin, A. P., & Allen, J. T. (2013). A review of the measurement and modelling of Dinoflagellate bioluminescence. Progress in Oceanography, 109, 117–129. https://doi.org/10.1016/j.pocean.2012.10.008
- ^ Valiadi, M., & Iglesias-Rodriguez, D. (2013). Understanding Bioluminescence in Dinoflagellates-How Far Have We Come?. Microorganisms, 1(1), 3–25. https://doi.org/10.3390/microorganisms1010003
External links
edit- Dinoflagellate+luciferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
