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Agmatine N4-coumaroyltransferase
In enzymology, an agmatine N4-coumaroyltransferase () is an enzyme that catalyzes the chemical reaction :4-coumaroyl-CoA + agmatine \rightleftharpoons CoA + N-(4-guanidinobutyl)-4-hydroxycinnamamide Thus, the two substrates of this enzyme are 4-coumaroyl-CoA and agmatine, whereas its two products are CoA and N-(4-guanidinobutyl)-4-hydroxycinnamamide. This enzyme belongs to the family of transferases, to be specific those acyltransferases transferring groups other than aminoacyl groups. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivial ... of this enzyme class is 4-coumaroyl-CoA:agmatine N4-coumaroyltransferase. Other names in common use include p-coumaroyl-CoA-agmatine N-p-coumaroyltransferase, agmatine coumaroyltransferase, and 4-coumaroyl-CoA:agmatine 4-N-cou ...
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Enzymology
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the 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 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 are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ...
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Enzyme
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the 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 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 are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ...
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Catalysis
Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recycles quickly, very small amounts of catalyst often suffice; mixing, surface area, and temperature are important factors in reaction rate. Catalysts generally react with one or more reactants to form intermediates that subsequently give the final reaction product, in the process of regenerating the catalyst. Catalysis may be classified as either homogeneous, whose components are dispersed in the same phase (usually gaseous or liquid) as the reactant, or heterogeneous, whose components are not in the same phase. Enzymes and other biocatalysts are often considered as a third category. Catalysis is ubiquitous in chemical industry of all kinds. Estimates are that 90% of all commercially produced chemical products involve catalysts at some s ...
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Chemical Reaction
A chemical reaction is a process that leads to the IUPAC nomenclature for organic transformations, chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the positions of electrons in the forming and breaking of chemical bonds between atoms, with no change to the Atomic nucleus, nuclei (no change to the elements present), and can often be described by a chemical equation. Nuclear chemistry is a sub-discipline of chemistry that involves the chemical reactions of unstable and radioactive Chemical element, elements where both electronic and nuclear changes can occur. The substance (or substances) initially involved in a chemical reaction are called reagent, reactants or reagents. Chemical reactions are usually characterized by a chemical change, and they yield one or more Product (chemistry), products, which usually have properties different from the reactants. Reactions often consist of a sequence o ...
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Substrate (biochemistry)
In chemistry, the term substrate is highly context-dependent. Broadly speaking, it can refer either to a chemical species being observed in a chemical reaction, or to a surface on which other chemical reactions or microscopy are performed. In the former sense, a reagent is added to the ''substrate'' to generate a product through a chemical reaction. The term is used in a similar sense in synthetic and organic chemistry, where the substrate is the chemical of interest that is being modified. In biochemistry, an enzyme substrate is the material upon which an enzyme acts. When referring to Le Chatelier's principle, the substrate is the reagent whose concentration is changed. ;Spontaneous reaction : :*Where S is substrate and P is product. ;Catalysed reaction : :*Where S is substrate, P is product and C is catalyst. In the latter sense, it may refer to a surface on which other chemical reactions are performed or play a supporting role in a variety of spectroscopic and microscop ...
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4-coumaroyl-CoA
Coumaroyl-coenzyme A is the thioester of coenzyme-A and coumaric acid. Coumaroyl-coenzyme A is a central intermediate in the biosynthesis of myriad natural products found in plants. These products include Monolignol, lignols (precursors to lignin and lignocellulose), flavonoids, isoflavonoids, coumarins, aurones, stilbenes, catechin, and other phenylpropanoids. Biosynthesis and significance It is generated in nature from phenylalanine, which is converted by Phenylalanine ammonia-lyase, PAL to trans-cinnamate. Trans-cinnamate is hydroxylated by trans-cinnamate 4-monooxygenase to give 4-hydroxycinnamate (i.e, coumarate). Coumarate is condensed with coenzyme-A in the presence of 4-coumarate-CoA ligase: :ATP + 4-coumarate + CoA \rightleftharpoons AMP + diphosphate + 4-coumaroyl-CoA. Enzymes using Coumaroyl-Coenzyme A * Anthocyanin 3-O-glucoside 6''-O-hydroxycinnamoyltransferase * Anthocyanin 5-aromatic acyltransferase * Chalcone synthase * 4-Coumarate-CoA ligase * 6'-Deoxychalcon ...
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Agmatine
Agmatine, also known as 4-aminobutyl-guanidine, is an aminoguanidine that was discovered in 1910 by Albrecht Kossel. Agmatine is a chemical substance which is naturally created from the amino acid arginine. Agmatine has been shown to exert modulatory action at multiple molecular targets, notably: neurotransmitter systems, ion channels, nitric oxide (NO) synthesis and polyamine metabolism and this provides bases for further research into potential applications. History Agmatine was discovered in 1910 by Albrecht Kossel. The term stems from A- (for amino-) + g- (from guanidine) + -ma- (from ptomaine) + -in (German)/-ine (English) suffix with insertion of -t- apparently for euphony. A year after its discovery, it was found that Agmatine could increase blood flow in rabbits; however, the physiological relevance of these findings were questioned given the high concentrations (high μM range) required. In the 1920s, researchers in the diabetes clinic of Oskar Minkowski have shown tha ...
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Product (chemistry)
Products are the species formed from chemical reactions. During a chemical reaction, reactants are transformed into products after passing through a high energy transition state. This process results in the consumption of the reactants. It can be a spontaneous reaction or mediated by catalysts which lower the energy of the transition state, and by solvents which provide the chemical environment necessary for the reaction to take place. When represented in chemical equations, products are by convention drawn on the right-hand side, even in the case of reversible reactions. The properties of products such as their energies help determine several characteristics of a chemical reaction, such as whether the reaction is exergonic or endergonic. Additionally, the properties of a product can make it easier to extract and purify following a chemical reaction, especially if the product has a different state of matter than the reactants. Spontaneous reaction : R \rightarrow P *Where R is r ...
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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 ...
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N-(4-guanidinobutyl)-4-hydroxycinnamamide
Chemistry * ''n-'', a lowercase prefix in chemistry denoting the straight-chain form of an open-chain compound In chemistry, an open-chain compound (also spelled as open chain compound) or acyclic compound (Greek prefix "α", ''without'' and "κύκλος", ''cycle'') is a compound with a linear structure, rather than a cyclic one. An open-chain compound ha ... in contrast to its branched isomer * ''N-'', an uppercase prefix in chemistry denoting that the substituent is bonded to the nitrogen, as in amines Mathematics, science and technology The italicized letter ''n'' is used in mathematics to denote an arbitrary number (usually a non-negative integer). * ''n''-ary associativity * ''n''-ary code * ''n''-ary group * ''n''-back * ''n''-body problem * ''n''-category * ''n''-category number * ''n''-connected space * ''n''-curve * ''n''-dimensional space * ''n''-dimensional sequential move puzzle * ''n''-electron valence state perturbation theory (NEVPT) * ''n''-entity * ...
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Transferase
A transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups (e.g. a methyl or glycosyl group) from one molecule (called the donor) to another (called the acceptor). They are involved in hundreds of different biochemical pathways throughout biology, and are integral to some of life's most important processes. Transferases are involved in myriad reactions in the cell. Three examples of these reactions are the activity of coenzyme A (CoA) transferase, which transfers thiol esters, the action of N-acetyltransferase, which is part of the pathway that metabolizes tryptophan, and the regulation of pyruvate dehydrogenase (PDH), which converts pyruvate to acetyl CoA. Transferases are also utilized during translation. In this case, an amino acid chain is the functional group transferred by a peptidyl transferase. The transfer involves the removal of the growing amino acid chain from the tRNA molecule in the A-site of the ribosome and its subse ...
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Acyltransferase
Acyltransferase is a type of transferase enzyme that acts upon acyl groups. Examples include: * Glyceronephosphate O-acyltransferase * Lecithin-cholesterol acyltransferase *Long-chain-alcohol O-fatty-acyltransferase In enzymology, a long-chain-alcohol O-fatty-acyltransferase () is an enzyme that catalyzes the chemical reaction :acyl-CoA + a long-chain alcohol \rightleftharpoons CoA + a long-chain ester Thus, the two substrates of this enzyme are acyl-C ... See also * Acetyltransferase External links * Transferases EC 2.3 {{2.3-enzyme-stub ...
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