Sandbox Reserved 1236: Difference between revisions
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== Function == | == Function == | ||
Luciferase is a class of bioluminescent enzymes that are found in several luminescence organisms. The most studied form Luciferase within its class is found in the North American Firefly (Photinus pyralis). This protein catalyzed the reaction that produces the distinctive yellow flash seen in from the abdomen of the insect. Photinus pyralis is known to use this mechanism for mate attraction and defense. Firefly Luciferase is unique to its species and different forms within the luciferase class can be found in other invertebrates and bacteria.<ref>Conti, E., Franks, N. P., & Brick, P. (1996). Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure, 4(3), 287-298.</ref>. The most notable being the bioluminescent enzyme found in Click Beetles (Pyrophorus). This protein is one of the most studied and widely used luminescence enzymes having various applications in cell and molecular biology. | Luciferase is a class of bioluminescent enzymes that are found in several luminescence organisms. The most studied form Luciferase within its class is found in the North American Firefly (Photinus pyralis). This protein catalyzed the reaction that produces the distinctive yellow flash seen in from the abdomen of the insect. Photinus pyralis is known to use this mechanism for mate attraction and defense. Firefly Luciferase is unique to its species and different forms within the luciferase class can be found in other invertebrates and bacteria.<ref>Conti, E., Franks, N. P., & Brick, P. (1996). Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure, 4(3), 287-298.</ref>. The most notable being the bioluminescent enzyme found in Click Beetles (Pyrophorus). This protein is one of the most studied and widely used luminescence enzymes having various applications in cell and molecular biology. | ||
Luciferase catalyzes two reactions; both reactions use an adenylation reaction along with ATP. The bioluminescent pathway produces Oxyluciferin and a photon of light. The other pathways does not produce light and is known as the nonluminescent reaction. This mechanism utilizes luciferin and produces Luciferyl-CoA. This addiotion of a CoA has been shown to be related to Acyl-CoA synthase used in the activation of fatty acids for oxidation. | |||
==Origin== | ==Origin== | ||
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A single peptide has been discover that plays a vital role in the photooxidation by Luciferase. The specific amino acid is a histidine located in the region 244HHGF247 of the protein <ref>Branchini, B. R., Magyar, R. A., Marcantonio, K. M., Newberry, K. J., Stroh, J. G., Hinz, L. K., & Murtiashaw, M. H. (1997). Identification of a Firefly Luciferase Active Site Peptide Using a Benzophenone-based Photooxidation Reagent. Journal of Biological Chemistry, 272(31), 19359-19364.</ref>. It has been shown to be necessary for the use of oxygen in the second part of the reaction | A single peptide has been discover that plays a vital role in the photooxidation by Luciferase. The specific amino acid is a histidine located in the region <scene name='75/750285/Luciferasemonomer114/2'>244HHGF247</scene> of the protein <ref>Branchini, B. R., Magyar, R. A., Marcantonio, K. M., Newberry, K. J., Stroh, J. G., Hinz, L. K., & Murtiashaw, M. H. (1997). Identification of a Firefly Luciferase Active Site Peptide Using a Benzophenone-based Photooxidation Reagent. Journal of Biological Chemistry, 272(31), 19359-19364.</ref>. It has been shown to be necessary for the use of oxygen in the second part of the reaction. | ||
==Applications== | ==Applications== | ||
