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Firefly Luciferase
Firefly luciferase is the light-emitting enzyme responsible for the bioluminescence of fireflies and click beetles. The enzyme catalyses the oxidation of firefly luciferin, requiring oxygen and ATP. Because of the requirement of ATP, firefly luciferases have been used extensively in biotechnology. Mechanism of reaction The chemical reaction catalyzed by firefly luciferase takes place in two steps: * luciferin + ATP → luciferyl adenylate + PPi * luciferyl adenylate + O2 → oxyluciferin + AMP + light Light is produced because the reaction forms oxyluciferin in an electronically excited state. The reaction releases a photon of light as oxyluciferin goes back to the ground state. Luciferyl adenylate can additionally participate in a side reaction with O2 to form hydrogen peroxide and dehydroluciferyl-AMP. About 20% of the luciferyl adenylate intermediate is oxidized in this pathway. Firefly luciferase generates light from luciferin in a multistep process. First, D-luci ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Luciferase Mechanism
Luciferase is a generic term for the class of oxidative enzymes that produce bioluminescence, and is usually distinguished from a photoprotein. The name was first used by Raphaël Dubois who invented the words ''luciferin'' and ''luciferase'', for the substrate and enzyme, respectively. Both words are derived from the Latin word ''lucifer'', meaning "lightbearer", which in turn is derived from the Latin words for "light" (''lux)'' and "to bring or carry" (''ferre)''.Luciferases are widely used in biotechnology, for bioluminescence imaging microscopy and as reporter genes, for many of the same applications as fluorescent proteins. However, unlike fluorescent proteins, luciferases do not require an external light source, but do require addition of luciferin, the consumable substrate. Examples A variety of organisms regulate their light production using different luciferases in a variety of light-emitting reactions. The majority of studied luciferases have been found in animals, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Luciferase
Luciferase is a generic term for the class of oxidative enzymes that produce bioluminescence, and is usually distinguished from a photoprotein. The name was first used by Raphaël Dubois who invented the words ''luciferin'' and ''luciferase'', for the substrate and enzyme, respectively. Both words are derived from the Latin word ''lucifer'', meaning "lightbearer", which in turn is derived from the Latin words for "light" (''lux)'' and "to bring or carry" (''ferre)''.Luciferases are widely used in biotechnology, for bioluminescence imaging microscopy and as reporter genes, for many of the same applications as fluorescent proteins. However, unlike fluorescent proteins, luciferases do not require an external light source, but do require addition of luciferin, the consumable substrate. Examples A variety of organisms regulate their light production using different luciferases in a variety of light-emitting reactions. The majority of studied luciferases have been found in animals, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Photinus Pyralis
''Photinus pyralis'', known by the common names common eastern firefly and big dipper firefly, is the most common species of firefly in North America. ''P. pyralis'' is a flying and light-producing beetle with a light organ on the ventral side of its abdomen. This organism is sometimes incorrectly classified as ''Photuris pyralis'', which likely results from mistaking the similar-sounding genus ''Photuris''. The ''Photuris'' female may also lure a ''Photinus pyralis'' to be eaten to obtain spider-repellent steroids called "Lucibufagin, lucibufagins". In males the light organ covers the entire ventral surface of the three most posterior segments and in females it only covers a portion of the third posterior segment.Mast, S.O. 1912. Behaviour of fire-flies (Photinus pyralis) with special references to the problem of orientation. 256-272 These fireflies are most noticeable around twilight, in the early part of the evening and hover close to the ground. The species' common name ref ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hydrogen Peroxide
Hydrogen peroxide is a chemical compound with the formula . In its pure form, it is a very pale blue liquid that is slightly more viscous than water. It is used as an oxidizer, bleaching agent, and antiseptic, usually as a dilute solution (3%–6% by weight) in water for consumer use, and in higher concentrations for industrial use. Concentrated hydrogen peroxide, or " high-test peroxide", decomposes explosively when heated and has been used as a propellant in rocketry. Hydrogen peroxide is a reactive oxygen species and the simplest peroxide, a compound having an oxygen–oxygen single bond. It decomposes slowly when exposed to light, and rapidly in the presence of organic or reactive compounds. It is typically stored with a stabilizer in a weakly acidic solution in a dark bottle to block light. Hydrogen peroxide is found in biological systems including the human body. Enzymes that use or decompose hydrogen peroxide are classified as peroxidases. Properties The boiling poi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
C-terminus
The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The convention for writing peptide sequences is to put the C-terminal end on the right and write the sequence from N- to C-terminus. Chemistry Each amino acid has a carboxyl group and an amine group. Amino acids link to one another to form a chain by a dehydration reaction which joins the amine group of one amino acid to the carboxyl group of the next. Thus polypeptide chains have an end with an unbound carboxyl group, the C-terminus, and an end with an unbound amine group, the N-terminus. Proteins are naturally synthesized starting from the N-terminus and ending at the C-terminus. Function C-terminal retention signals While the N-terminus of a protein often c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
N-terminus
The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH2) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid, making it a chain. That leaves a free carboxylic group at one end of the peptide, called the C-terminus, and a free amine group on the other end called the N-terminus. By convention, peptide sequences are written N-terminus to C-terminus, left to right (in LTR writing systems). This correlates the translation direction to the text direction, because when a protein is translated from messenger RNA, it is created from the N-terminus to the C-terminus, as amino acids are added to the carboxyl end of the protein. Chemistry Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Domain
In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins. Background The concept of the domain was first proposed in 1973 by Wetlaufer aft ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Beta Oxidation
In biochemistry and metabolism, beta-oxidation is the catabolic process by which fatty acid molecules are broken down in the cytosol in prokaryotes and in the mitochondria in eukaryotes to generate acetyl-CoA, which enters the citric acid cycle, and NADH and FADH2, which are co-enzymes used in the electron transport chain. It is named as such because the beta carbon of the fatty acid undergoes oxidation to a carbonyl group. Beta-oxidation is primarily facilitated by the mitochondrial trifunctional protein, an enzyme complex associated with the inner mitochondrial membrane, although very long chain fatty acids are oxidized in peroxisomes. The overall reaction for one cycle of beta oxidation is: :C''n''-acyl-CoA + FAD + + + CoA → C''n''-2-acyl-CoA + + NADH + + acetyl-CoA Activation and membrane transport Free fatty acids cannot penetrate any biological membrane due to their negative charge. Free fatty acids must cross the cell membrane through specific transport pro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fatty Acid
In chemistry, particularly in biochemistry, a fatty acid is a carboxylic acid with an aliphatic chain, which is either saturated or unsaturated. Most naturally occurring fatty acids have an unbranched chain of an even number of carbon atoms, from 4 to 28. Fatty acids are a major component of the lipids (up to 70% by weight) in some species such as microalgae but in some other organisms are not found in their standalone form, but instead exist as three main classes of esters: triglycerides, phospholipids, and cholesteryl esters. In any of these forms, fatty acids are both important dietary sources of fuel for animals and important structural components for cells. History The concept of fatty acid (''acide gras'') was introduced in 1813 by Michel Eugène Chevreul, though he initially used some variant terms: ''graisse acide'' and ''acide huileux'' ("acid fat" and "oily acid"). Types of fatty acids Fatty acids are classified in many ways: by length, by saturation vs unsaturati ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Long-chain-fatty-acid—CoA Ligase
The long chain fatty acyl-CoA ligase (or synthetase) is an enzyme () of the ligase family that activates the oxidation of complex fatty acids. Long chain fatty acyl-CoA synthetase catalyzes the formation of fatty acyl-CoA by a two-step process proceeding through an adenylation, adenylated intermediate. The enzyme catalyzes the following reaction, :Fatty acid + coenzyme A, CoA + adenosine triphosphate, ATP ⇌ Acyl-CoA + adenosine monophosphate, AMP + pyrophosphate, PPi It is present in all organisms from bacteria to humans. It catalyzes the pre-step reaction for β-oxidation of fatty acids or can be incorporated in phospholipids. Function Long chain fatty acyl-CoA synthetase, LC-FACS, plays a role in the physiological regulation of various cellular functions via the production of long chain fatty acyl-CoA esters, which reportedly have affected protein transport, enzyme activation, protein acylation, cell signaling, and transcriptional regulation. The formation of fatty acyl-Co ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Coenzyme A
Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle. All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester) as a substrate. In humans, CoA biosynthesis requires cysteine, pantothenic acid, pantothenate (vitamin B5), and adenosine triphosphate (ATP). In acetyl-CoA, its acetyl form, coenzyme A is a highly versatile molecule, serving metabolic functions in both the Anabolism, anabolic and Catabolism, catabolic pathways. Acetyl-CoA is utilised in the post-translational regulation and allosteric regulation of pyruvate dehydrogenase and carboxylase to maintain and support the partition of Pyruvic acid, pyruvate synthesis and degradation. Discovery of structure Coenzyme A was identified by Fritz Lipmann in 1946, who also later gave it its name. Its structure was determined during the e ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
