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Dihydrolipoamide Dehydrogenase
Dihydrolipoamide dehydrogenase (DLD), also known as dihydrolipoyl dehydrogenase, mitochondrial, is an enzyme that in humans is encoded by the ''DLD'' gene. DLD is a flavoprotein enzyme that oxidizes dihydrolipoamide to lipoamide. Dihydrolipoamide dehydrogenase (DLD) is a mitochondrial enzyme that plays a vital role in energy metabolism in eukaryotes. This enzyme is required for the complete reaction of at least five different multi-enzyme complexes. Additionally, DLD is a flavoenzyme oxidoreductase that contains a reactive disulfide bridge and a FAD cofactor that are directly involved in catalysis. The enzyme associates into tightly bound homodimers required for its enzymatic activity. File:Lipoamide-2D-skeletal.png, Lipoamide File:Dihydrolipoamide.svg, Dihydrolipoamide Structure The protein encoded by the DLD gene comes together with another protein to form a dimer in the central metabolic pathway. Several amino acids within the catalytic pocket have been identified ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme
An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different molecules known as product (chemistry), products. Almost all metabolism, metabolic processes in the cell (biology), cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme, pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts include Ribozyme, catalytic RNA molecules, also called ribozymes. They are sometimes descr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Active Site
In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of amino acid residues that form temporary bonds with the substrate, the ''binding site'', and residues that catalyse a reaction of that substrate, the ''catalytic site''. Although the active site occupies only ~10–20% of the volume of an enzyme, it is the most important part as it directly catalyzes the chemical reaction. It usually consists of three to four amino acids, while other amino acids within the protein are required to maintain the tertiary structure of the enzymes. Each active site is evolved to be optimised to bind a particular substrate and catalyse a particular reaction, resulting in high specificity. This specificity is determined by the arrangement of amino acids within the active site and the structure of the substrates. Sometimes enzymes also need to bind with some cofactors to fulfil their functio ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Failure To Thrive
Failure to thrive (FTT), also known as weight faltering or faltering growth, indicates insufficient weight gain or absence of appropriate physical growth in children. FTT is usually defined in terms of weight, and can be evaluated either by a low weight for the child's age, or by a low rate of increase in the weight. The term "failure to thrive" has been used in different ways, as no single objective standard or universally accepted definition exists for when to diagnose FTT. One definition describes FTT as a fall in one or more weight centile spaces on a World Health Organization (WHO) growth chart depending on birth weight or when weight is below the 2nd percentile of weight for age irrespective of birth weight. Another definition of FTT is a weight for age that is consistently below the fifth percentile or weight for age that falls by at least two major percentile lines on a growth chart. While weight loss after birth is normal and most babies return to their birth weight by t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Reperfusion Injury
Reperfusion injury, sometimes called ischemia-reperfusion injury (IRI) or reoxygenation injury, is the tissue damage caused when blood supply returns to tissue ('' re-'' + ''perfusion'') after a period of ischemia or lack of oxygen (anoxia or hypoxia). The absence of oxygen and nutrients from blood during the ischemic period creates a condition in which the restoration of circulation results in inflammation and oxidative damage through the induction of oxidative stress rather than (or along with) restoration of normal function. Reperfusion injury is distinct from cerebral hyperperfusion syndrome (sometimes called "Reperfusion syndrome"), a state of abnormal cerebral vasodilation. Mechanisms Reperfusion of ischemic tissues is often associated with microvascular injury, particularly due to increased permeability of capillaries and arterioles that lead to an increase of diffusion and fluid filtration across the tissues. Activated endothelial cells produce more reactive oxygen sp ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Moonlighting
Protein moonlighting is a phenomenon by which a protein can perform more than one function. It is an example ogene sharing Ancestral moonlighting proteins originally possessed a single function but, through evolution, acquired additional functions. Many proteins that moonlight are enzymes; others are receptors, ion channels or chaperones. The most common primary function of moonlighting proteins is enzymatic catalysis, but these enzymes have acquired secondary non-enzymatic roles. Some examples of functions of moonlighting proteins secondary to catalysis include signal transduction, transcriptional regulation, apoptosis, motility, and structural. Protein moonlighting occurs widely in nature. Protein moonlighting through gene sharing differs from the use of a single gene to generate different proteins by alternative RNA splicing, DNA rearrangement, or post-translational processing. It is also different from the multifunctionality of the protein, in which the protein has mult ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hydroxyl Radical
The hydroxyl radical, •HO, is the neutral form of the hydroxide ion (HO–). Hydroxyl radicals are highly reactive and consequently short-lived; however, they form an important part of radical chemistry. Most notably hydroxyl radicals are produced from the decomposition of hydroperoxides (ROOH) or, in atmospheric chemistry, by the reaction of excited atomic oxygen with water. It is also an important radical formed in radiation chemistry, since it leads to the formation of hydrogen peroxide and oxygen, which can accelerate corrosion and stress corrosion cracking in coolant systems subjected to radioactive environments. Hydroxyl radicals are also produced during UV-light dissociation of hydrogen peroxide (H2O2) (suggested in 1879) and likely in Fenton chemistry, where trace amounts of reduced transition metals catalyze peroxide-mediated oxidations of organic compounds. In organic synthesis, hydroxyl radicals are most commonly generated by photolysis of '' 1-Hydroxy-2(1H ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ferrous
In chemistry, iron(II) refers to the chemical element, element iron in its +2 oxidation number, oxidation state. The adjective ''ferrous'' or the prefix ''ferro-'' is often used to specify such compounds, as in ''ferrous chloride'' for iron(II) chloride (). The adjective ''ferric'' is used instead for iron(III) salts, containing the cation Fe3+. The word ''wikt:ferrous, ferrous'' is derived from the Latin word , meaning "iron". In salt (chemistry), ionic compounds (salts), such an atom may occur as a separate cation (positive ion) abbreviated as Fe2+, although more precise descriptions include other ligands such as water and halides. Iron(II) centres occur in coordination complexes, such as in the anion ferrocyanide, , where six cyanide ligands are bound the metal centre; or, in organometallic compounds, such as the ferrocene , where two cyclopentadienyl anions are bound to the FeII centre. Ferrous ions in biology All known forms of life require iron. Many proteins in living ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Superoxide
In chemistry, a superoxide is a compound that contains the superoxide ion, which has the chemical formula . The systematic name of the anion is dioxide(1−). The reactive oxygen ion superoxide is particularly important as the product of the one-electron reduction of dioxygen , which occurs widely in nature. Molecular oxygen (dioxygen) is a diradical containing two unpaired electrons, and superoxide results from the addition of an electron which fills one of the two degenerate molecular orbitals, leaving a charged ionic species with a single unpaired electron and a net negative charge of −1. Both dioxygen and the superoxide anion are free radicals that exhibit paramagnetism. Superoxide was historically also known as "hyperoxide". Salts Superoxide forms salts with alkali metals and alkaline earth metals. The salts sodium superoxide (), potassium superoxide (), rubidium superoxide () and caesium superoxide () are prepared by the reaction of with the respect ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ubiquinone
Coenzyme Q10 (CoQ10 ), also known as ubiquinone, is a naturally occurring Cofactor (biochemistry), biochemical cofactor (coenzyme) and an antioxidant produced by the human body. It can also be obtained from dietary sources, such as meat, fish, seed oils, vegetables, and dietary supplements. CoQ10 is found in many organisms, including animals and bacteria. CoQ10 plays a role in mitochondrial oxidative phosphorylation, aiding in the production of adenosine triphosphate (ATP), which is involved in energy transfer within cells. The structure of CoQ10 consists of a benzoquinone moiety and an isoprenoid side chain, with the "10" referring to the number of Isoprene, isoprenyl chemical subunits in its tail. Although a ubiquitous molecule in human tissues, CoQ10 is not a dietary nutrient and does not have a Dietary Reference Intake, recommended intake level, and its use as a supplement is not approved drug, approved in the United States for any health or anti-disease effect. Biologica ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nitric Oxide
Nitric oxide (nitrogen oxide, nitrogen monooxide, or nitrogen monoxide) is a colorless gas with the formula . It is one of the principal oxides of nitrogen. Nitric oxide is a free radical: it has an unpaired electron, which is sometimes denoted by a dot in its chemical formula (•N=O or •NO). Nitric oxide is also a heteronuclear diatomic molecule, a class of molecules whose study spawned early modern theories of chemical bonding. An important intermediate in industrial chemistry, nitric oxide forms in combustion systems and can be generated by lightning in thunderstorms. In mammals, including humans, nitric oxide is a signaling molecule in many physiological and pathological processes. It was proclaimed the " Molecule of the Year" in 1992. The 1998 Nobel Prize in Physiology or Medicine was awarded for discovering nitric oxide's role as a cardiovascular signalling molecule. Its impact extends beyond biology, with applications in medicine, such as the development of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ferric
In chemistry, iron(III) or ''ferric'' refers to the chemical element, element iron in its +3 oxidation number, oxidation state. ''Ferric chloride'' is an alternative name for iron(III) chloride (). The adjective ''ferrous'' is used instead for iron(II) salts, containing the cation Fe2+. The word ''wikt:ferric, ferric'' is derived from the Latin word , meaning "iron". Although often abbreviated as Fe3+, that naked ion does not exist except under extreme conditions. Iron(III) centres are found in many compounds and coordination complexes, where Fe(III) is bonded to several Ligand, ligands. A molecular ferric complex is the anion ferrioxalate, , with three bidentate oxalate ions surrounding the Fe core. Relative to lower oxidation states, ferric is less common in organoiron chemistry, but the ferrocenium cation is well known. Iron(III) in biology All known forms of life require iron, which usually exists in Fe(II) or Fe(III) oxidation states. Many proteins in living beings cont ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Diaphorase
Diaphorase may refer to: * Cytochrome b5 reductase, an enzyme * NADH dehydrogenase NADH dehydrogenase is an enzyme that converts nicotinamide adenine dinucleotide (NAD) from its reduced form (NADH) to its oxidized form (NAD+). Members of the NADH dehydrogenase family and analogues are commonly systematically named using the f ..., an enzyme * NADPH dehydrogenase, an enzyme See also * NADPH-diaphorase (other) {{Short pages monitor ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
