Luciferase
(Redirected from Luciferases)
Luciferase is a generic term for the class of oxidative enzymes that produce bioluminescence, and is usually distinguished from a photoprotein. The name is derived from lucifer, the Latin word for "light-bringer". Luciferases are widely used in biotechnology, particularly in the field of molecular biology.
Biochemistry[edit | edit source]
Luciferases catalyze the oxidation of a luciferin substrate, resulting in the emission of light. The reaction typically requires adenosine triphosphate (ATP) and produces oxyluciferin, light, and other byproducts. The specific wavelength (color) of the emitted light depends on the structure of the luciferin and the luciferase enzyme.
Types of Luciferase[edit | edit source]
There are several types of luciferase, each derived from different organisms and with different properties:
- Firefly luciferase (from the firefly species Photinus pyralis) is one of the most well-known and widely used luciferases in research.
- Renilla luciferase (from the sea pansy Renilla reniformis) is another commonly used luciferase, particularly in reporter gene assays.
- Bacterial luciferase (from the Vibrio species of bacteria) is used in various biotechnological applications.
Applications[edit | edit source]
Luciferases have a wide range of applications in scientific research and biotechnology:
- Reporter genes: Luciferase genes are often used as reporter genes in genetic engineering to monitor the expression of other genes.
- Bioluminescent imaging: Luciferase enzymes are used in bioluminescent imaging to study biological processes in live animals.
- ATP detection: Luciferase-based assays are used to detect the presence of ATP, which is an indicator of cell viability and metabolic activity.
Mechanism of Action[edit | edit source]
The general mechanism of action for luciferases involves the binding of luciferin and oxygen to the enzyme, followed by the oxidation of luciferin. This reaction releases energy in the form of light. The specific steps and intermediates can vary between different types of luciferases.
History[edit | edit source]
The discovery of luciferase dates back to the 19th century when Raphaël Dubois first identified the enzyme in fireflies. Since then, luciferases have been isolated from various organisms and have become invaluable tools in scientific research.
See also[edit | edit source]
References[edit | edit source]
External links[edit | edit source]
Search WikiMD
Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro / Zepbound) available.
Advertise on WikiMD
WikiMD's Wellness Encyclopedia |
Let Food Be Thy Medicine Medicine Thy Food - Hippocrates |
Translate this page: - East Asian
中文,
日本,
한국어,
South Asian
हिन्दी,
தமிழ்,
తెలుగు,
Urdu,
ಕನ್ನಡ,
Southeast Asian
Indonesian,
Vietnamese,
Thai,
မြန်မာဘာသာ,
বাংলা
European
español,
Deutsch,
français,
Greek,
português do Brasil,
polski,
română,
русский,
Nederlands,
norsk,
svenska,
suomi,
Italian
Middle Eastern & African
عربى,
Turkish,
Persian,
Hebrew,
Afrikaans,
isiZulu,
Kiswahili,
Other
Bulgarian,
Hungarian,
Czech,
Swedish,
മലയാളം,
मराठी,
ਪੰਜਾਬੀ,
ગુજરાતી,
Portuguese,
Ukrainian
Medical Disclaimer: WikiMD is not a substitute for professional medical advice. The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes. Please consult your health care provider before making any healthcare decisions or for guidance about a specific medical condition. WikiMD expressly disclaims responsibility, and shall have no liability, for any damages, loss, injury, or liability whatsoever suffered as a result of your reliance on the information contained in this site. By visiting this site you agree to the foregoing terms and conditions, which may from time to time be changed or supplemented by WikiMD. If you do not agree to the foregoing terms and conditions, you should not enter or use this site. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.
Contributors: Prab R. Tumpati, MD