Hyperphosphorylation
Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or otherwise modifying its function. Approximately 13,000 human proteins have sites that are phosphorylated. The reverse reaction of phosphorylation is called dephosphorylation, and is catalyzed by protein phosphatases. Protein kinases and phosphatases work independently and in a balance to regulate the function of proteins. The amino acids most commonly phosphorylated are serine, threonine, tyrosine, and histidine. These phosphorylations play important and well-characterized roles in signaling pathways and metabolism. However, other amino acids can also be phosphorylated post-translationally, including arginine, lysine, aspartic acid, glutamic acid and cysteine, a ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Phosphorylated Serine
Phosphoserine (abbreviated as SEP or J) is an ester of serine and phosphoric acid. Phosphoserine is a component of many proteins as the result of posttranslational modifications. The phosphorylation of the alcohol functional group in serine to produce phosphoserine is catalyzed by various types of kinases. Through the use of technologies that utilize an expanded genetic code, phosphoserine can also be incorporated into proteins during translation. It is a normal metabolite In biochemistry, a metabolite is an intermediate or end product of metabolism. The term is usually used for small molecules. Metabolites have various functions, including fuel, structure, signaling, stimulatory and inhibitory effects on enzymes, c ... found in human biofluids. Phosphoserine has three potential coordination sites (carboxyl, amine and phosphate group) Determination of the mode of coordination between phosphorylated ligands and metal ions occurring in an organism is a first step to explain the fu ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Glutamic Acid
Glutamic acid (symbol Glu or E; known as glutamate in its anionic form) is an α- amino acid that is used by almost all living beings in the biosynthesis of proteins. It is a non-essential nutrient for humans, meaning that the human body can synthesize enough for its use. It is also the most abundant excitatory neurotransmitter in the vertebrate nervous system. It serves as the precursor for the synthesis of the inhibitory gamma-aminobutyric acid (GABA) in GABAergic neurons. Its molecular formula is . Glutamic acid exists in two optically isomeric forms; the dextrorotatory -form is usually obtained by hydrolysis of gluten or from the waste waters of beet-sugar manufacture or by fermentation.Webster's Third New International Dictionary of the English Language Unabridged, Third Edition, 1971. Its molecular structure could be idealized as HOOC−CH()−()2−COOH, with two carboxyl groups −COOH and one amino group −. However, in the solid state and mildly acidic water s ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Pyruvate Dehydrogenase Complex
Pyruvate dehydrogenase complex (PDC) is a complex of three enzymes that converts pyruvate into acetyl-CoA by a process called pyruvate decarboxylation. Acetyl-CoA may then be used in the citric acid cycle to carry out cellular respiration, and this complex links the glycolysis metabolic pathway to the citric acid cycle. Pyruvate decarboxylation is also known as the "pyruvate dehydrogenase reaction" because it also involves the oxidation of pyruvate. The levels of pyruvate dehydrogenase enzymes play a major role in regulating the rate of carbohydrate metabolism and are strongly stimulated by the evolutionarily ancient hormone insulin. The PDC is opposed by the activity of pyruvate dehydrogenase kinase, and this mechanism plays a pivotal role in regulating rates of carbohydrate and lipid metabolism in many physiological states across taxa, including feeding, starvation, diabetes mellitus, hyperthyroidism, and hibernation. The multi-enzyme complex is related structurally and fun ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Glycogenolysis
Glycogenolysis is the breakdown of glycogen (n) to glucose-1-phosphate and glycogen (n-1). Glycogen branches are catabolized by the sequential removal of glucose monomers via phosphorolysis, by the enzyme glycogen phosphorylase. Mechanism In the muscles, glycogenolysis begins due to the binding of cAMP to phosphorylate kinase, converting the latter to its active form so it can convert phosphorylase b to phosphorylase a, which is responsible for catalyzing the breakdown of glycogen. The overall reaction for the breakdown of glycogen to glucose-1-phosphate is: : glycogen(n residues) + Pi glycogen(n-1 residues) + glucose-1-phosphate Here, glycogen phosphorylase cleaves the bond linking a terminal glucose residue to a glycogen branch by substitution of a phosphoryl group for the α →4linkage. Glucose-1-phosphate is converted to glucose-6-phosphate (which often ends up in glycolysis) by the enzyme phosphoglucomutase. Glucose residues are phosphorolysed from bra ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Adenanthos Cuneatus
''Adenanthos cuneatus'', also known as coastal jugflower, flame bush, bridle bush and sweat bush, is a shrub of the family Proteaceae, native to the south coast of Western Australia. The French naturalist Jacques Labillardière originally described it in 1805. Within the genus ''Adenanthos'', it lies in the Section (botany), section ''Adenanthos sect. Adenanthos, Adenanthos'' and is most closely related to ''Adenanthos stictus, A. stictus''. ''A. cuneatus'' has hybridized with four other species of ''Adenanthos''. Growing to high and wide, it is erect to prostrate in Habit (biology), habit, with wedge-shaped lobed leaves covered in fine silvery hair. The single red flowers are insignificant, and appear all year, though especially in late spring. The reddish new growth occurs over the summer. It is sensitive to ''Phytophthora cinnamomi'' Root rot, dieback, hence requiring a sandy soil and good drainage to grow in cultivation, its natural habitat of sandy soils in heathlan ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Earl Wilbur Sutherland Jr
Earl Wilbur Sutherland Jr. (November 19, 1915 – March 9, 1974) was an American pharmacologist and biochemist born in Burlingame, Kansas. Sutherland won a Nobel Prize in Physiology or Medicine in 1971 "for his discoveries concerning the mechanisms of the action of hormones", especially epinephrine, via second messengers, namely cyclic adenosine monophosphate, or cyclic AMP. Early life and education Sutherland was born on November 19, 1915, in Burlingame, Kansas. The second youngest of six children, he was raised by his mother, Edith M. Hartshorn, and his father, Earl W. Sutherland.Gale Group (2006)"World of Scientific Discovery on Earl Sutherland". World of Scientific Discovery. Though his father, who was originally from Wisconsin, had attended Grinnell College for two years, he ultimately led an agrarian lifestyle that took him to both New Mexico and Oklahoma before settling down in Burlingame to raise a family. Edith, a Missouri native, had some training in nursing at what wa ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Edwin G
The name Edwin means "wealth-friend". It comes from (wealth, good fortune) and (friend). Thus the Old English form is Ēadwine, a name widely attested in early medieval England. Edwina is the feminine form of the name. Notable people and characters with the name include: Historical figures * Edwin of Northumbria (died 632 or 633), King of Northumbria and Christian saint * Edwin (son of Edward the Elder) (died 933) * Eadwine of Sussex (died 982), Ealdorman of Sussex * Eadwine of Abingdon (died 990), Abbot of Abingdon * Edwin, Earl of Mercia (died 1071), brother-in-law of Harold Godwinson (Harold II) * Edwin Sandys (bishop) (1519–1588), Archbishop of York Modern era * E. W. Abeygunasekera, Sri Lankan Sinhala politician * Edwin Abbott Abbott (1838–1926), English schoolmaster, theologian, and Anglican priest * Edwin Ariyadasa (1922–2021), Sri Lankan Sinhala journalist * Edwin Arrieta Arteaga (died 2023), Colombian murder victim * Edwin Austin Abbey (1852–1 ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Edmond H
Edmond may refer to: Arts and entertainment * ''Edmond'' (play), a 1982 play by David Mamet ** ''Edmond'' (film), a 2005 film based on the 1982 play * '' E.d.M.O.N.D'', a 2013 EP by Edmond Leung * ''Edmond'', a 2016 play by Alexis Michalik ** ''Edmond'', a 2019 film adaptation of the play, written and directed by Michalik * Berlin Edmond (born 1992), American YouTuber known online as Berleezy Places * Edmond, Kansas * Edmond, Oklahoma * Edmonds, Washington * Edmond, West Virginia Others * Edmond (given name) * ''Edmond'' (1833), a passenger sailing ship that sank off the coast of Ireland in 1850 * Edmond, a racehorse that was the joint favourite for the 2001 Grand National See also *Edmund (other) *Edward (other) Edward is an English given name. Edward may also refer to: * ''Edward'' (ballad), a traditional murder ballad * ''Edward'' (EP), by British singer-songwriter Emmy the Great * Edward (mango), a mango cultivar * Lake Edward Lake Edward (locally ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Glycogen Phosphorylase
Glycogen phosphorylase is one of the phosphorylase enzymes (). Glycogen phosphorylase catalyzes the rate-limiting step in glycogenolysis in animals by releasing glucose-1-phosphate from the terminal alpha-1,4-glycosidic bond. Glycogen phosphorylase is also studied as a model protein regulated by both reversible phosphorylation and allosteric effects. Mechanism Glycogen phosphorylase breaks up glycogen into glucose subunits (see also figure below): (α-1,4 glycogen chain)n + Pi ⇌ (α-1,4 glycogen chain)n-1 + α-D-glucose-1-phosphate. Glycogen is left with one fewer glucose molecule, and the free glucose molecule is in the form of glucose-1-phosphate. In order to be used for metabolism, it must be converted to glucose-6-phosphate by the enzyme phosphoglucomutase. Although the reaction is reversible in vitro, within the cell the enzyme only works in the forward direction as shown below because the concentration of inorganic phosphate is much higher than that of gluco ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Phosphorylase
In biochemistry, phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate+hydrogen) to an acceptor. :A-B + P A + P-B They include allosteric enzymes that catalyze the production of glucose-1-phosphate from a glucan such as glycogen, starch or maltodextrin. Phosphorylase is also a common name used for glycogen phosphorylase in honor of Earl W. Sutherland Jr., who in the late 1930s discovered it as the first phosphorylase. Function Phosphorylases should not be confused with phosphatases, which remove phosphate groups. In more general terms, phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate + hydrogen) to an acceptor, not to be confused with a phosphatase (a hydrolase) or a kinase (a phosphotransferase). A phosphatase removes a phosphate group from a donor using water, whereas a kinase transfers a phosphate group from a donor (usually ATP) to an accep ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Casein
Casein ( , from Latin ''caseus'' "cheese") is a family of related phosphoproteins (CSN1S1, αS1, aS2, CSN2, β, K-casein, κ) that are commonly found in mammalian milk, comprising about 80% of the proteins in cow's milk and between 20% and 60% of the proteins in breast milk, human milk. Sheep's milk, Sheep and cow milk have a higher casein content than other types of milk with human milk having a particularly low casein content. Casein is the primary emulsifier in milk, that is, it helps in mixing oils, fats, and water in milk. Casein has a wide variety of uses, from being a major component of cheese, to use as a food additive. The most common form of casein is sodium caseinate (historically called nutrose), which is a very efficient emulsifier. Casein is secreted into milk from mammary cells in the form of colloidal casein micelles, a type of biomolecular condensate. As a food source, casein supplies amino acids, carbohydrates, and two essential elements, calcium and phosphoru ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Protein Kinase
A protein kinase is a kinase which selectively modifies other proteins by covalently adding phosphates to them ( phosphorylation) as opposed to kinases which modify lipids, carbohydrates, or other molecules. Phosphorylation usually results in a functional change of the target protein ( substrate) by changing enzyme activity, cellular location, or association with other proteins. The human genome contains about 500 protein kinase genes and they constitute about 2% of all human genes. There are two main types of protein kinase. The great majority are serine/threonine kinases, which phosphorylate the hydroxyl groups of serines and threonines in their targets. Most of the others are tyrosine kinases, although additional types exist. Protein kinases are also found in bacteria and plants. Up to 30% of all human proteins may be modified by kinase activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction. Chemical ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |