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Arogenate
Arogenic acid is an Metabolic intermediate, intermediate in the biosynthesis of phenylalanine and tyrosine. At physiological pH it exists as its conjugate base arogenate as the acid form is unstable. Metabolism Arogenate is synthesized from prephenate by transamination. This reaction can be catalyzed by several enzymes, including aromatic-amino-acid transaminase, aspartate—prephenate aminotransferase and Aspartate—prephenate aminotransferase, glutamate—prephenate aminotransferase: : prephenate + amino acid → arogenate + keto acid The amino acid in this case can be either aspartate or glutamate, which turn into oxaloacetate and 2-oxoglutarate, respectively. Arogenate is then turned into either phenylalanine or tyrosine. When prephenate dehydratase or arogenate dehydratase act upon arogenate, phenylalanine is produced: : arogenate → phenylalanine + H2O + CO2 When arogenate dehydrogenase, arogenate dehydrogenase (NAD(P)+) or arogenate dehydrogenase (NADP+) acts upon a ...
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Arogenate Dehydratase
Arogenate dehydratase (ADT) () is an enzyme that catalyzes the chemical reaction : L-arogenate → L phenylalanine + H2O + CO2 Certain forms of the protein have the potential to catalyze a second reaction, :L-prephenate → L-phenylpyruvate + H2O + CO2 This enzyme participates in phenylalanine, tyrosine, and tryptophan biosynthesis (an example structure is shown to the right. Nomenclature This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The List of enzymes, systematic name of this enzyme class is L-arogenate hydro-lyase (decarboxylating; L-phenylalanine-forming). Other names in common use include: * arogenate dehydratase * L-arogenate hydro-lyase (decarboxylating) * cyclohexadienyl dehydratase * carbocyclohexadienyl dehydratase * pheC * ADT Reaction The Carboxyl group, carboxyl and Hydroxide group, hydroxide groups (shown in red) attached to the 2,5-cyclohexene ring are eliminated from L-arogenate, leaving as carb ...
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Arogenate Dehydrogenase (NADP+)
In enzymology, an arogenate dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction :L-arogenate + NADP+ \rightleftharpoons L-tyrosine + NADPH + CO2 Thus, the two substrates of this enzyme are L-arogenate and NADP+, whereas its 3 products are L-tyrosine, NADPH, and CO2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. 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 semitrivi ... of this enzyme class is L-arogenate:NADP+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), pretyrosine dehydrogenase (ambiguous), TyrAAT1, TyrAAT2, and TyrAa. References * * * * EC 1.3.1 NADPH-dependent enzymes Enzy ...
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Arogenate Dehydrogenase
In enzymology, an arogenate dehydrogenase () is an enzyme that catalyzes the chemical reaction :L-arogenate + NAD+ \rightleftharpoons L-tyrosine + NADH + CO2 Thus, the two substrates of this enzyme are L-arogenate and NAD+, whereas its 3 products are L-tyrosine, NADH, and CO2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-arogenate:NAD+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), cyclohexadienyl dehydrogenase, pretyrosine dehydrogenase (ambiguous), and L-arogenate:NAD+ oxidoreductase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and novobiocin biosynthesis. Structural studies As of late 2007, only one structure A structure is an arrangement and organization of interrelated elements in a material object or system, or the object or system ...
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Arogenate Dehydrogenase (NAD(P)+)
In enzymology, an arogenate dehydrogenase AD(P)+'' () is an enzyme that catalyzes the chemical reaction :L-arogenate + NAD(P)+ \rightleftharpoons L-tyrosine + NAD(P)H + CO2 The 3 substrates of this enzyme are L-arogenate, NAD+, and NADP+, whereas its 4 products are L-tyrosine, NADH, NADPH, and CO2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. 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 semitrivi ... of this enzyme class is L-arogenate:NAD(P)+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), cyclohexadienyl dehydrogenase, and pretyrosine dehydrogenase (ambiguous). References * * EC 1.3.1 NADPH-dependent ...
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Aspartate—prephenate Aminotransferase
In enzymology, an aspartate-prephenate aminotransferase () is an enzyme that catalyzes the chemical reaction :L-arogenate + oxaloacetate \rightleftharpoons prephenate + L-aspartate Thus, the two substrates of this enzyme are L-arogenate and oxaloacetate, whereas its two products are prephenate and L-aspartate. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous 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 semitrivi ... of this enzyme class is L-arogenate:oxaloacetate aminotransferase. Other names in common use include prephenate transaminase (ambiguous), PAT (ambiguous), prephenate aspartate aminotransferase, and L-aspartate:prephenate aminotransferase. References * EC 2.6.1 Enzymes of unk ...
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Zwitterion
In chemistry, a zwitterion ( ; ), also called an inner salt or dipolar ion, is a molecule that contains an equal number of positively and negatively charged functional groups. : (1,2- dipolar compounds, such as ylides, are sometimes excluded from the definition.) Some zwitterions, such as amino acid zwitterions, are in chemical equilibrium with an uncharged "parent" molecule. Betaines are zwitterions that cannot isomerize to an all-neutral form, such as when the positive charge is located on a quaternary ammonium group. Similarly, a molecule containing a phosphonium group and a carboxylate group cannot isomerize. Amino acids Tautomerism of amino acids follows this stoichiometry: : The ratio of the concentrations of the two species in solution is independent of pH. It has been suggested, on the basis of theoretical analysis, that the zwitterion is stabilized in aqueous solution by hydrogen bonding with solvent water molecules. Analysis of neutron diffraction data for g ...
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Oxaloacetate
Oxaloacetic acid (also known as oxalacetic acid or OAA) is a crystalline organic compound with the chemical formula HO2CC(O)CH2CO2H. Oxaloacetic acid, in the form of its conjugate base oxaloacetate, is a metabolic intermediate in many processes that occur in animals. It takes part in gluconeogenesis, the urea cycle, the glyoxylate cycle, amino acid synthesis, fatty acid synthesis and the citric acid cycle. Properties Oxaloacetic acid undergoes successive deprotonations to give the dianion: :HO2CC(O)CH2CO2H −O2CC(O)CH2CO2H + H+, pKa = 2.22 :−O2CC(O)CH2CO2H −O2CC(O)CH2CO2− + H+, pKa = 3.89 At high pH, the enolizable proton is ionized: :−O2CC(O)CH2CO2− −O2CC(O−)CHCO2− + H+, pKa = 13.03 The enol forms of oxaloacetic acid are particularly stable. Keto-enol tautomerization is catalyzed by the enzyme oxaloacetate tautomerase. ''trans''-Enol-oxaloacetate also appears when tartrate is the substrate for fumarase. Biosynthesis Oxaloacetate forms ...
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Prephenate Dehydratase
The enzyme prephenate dehydratase () catalyzes the chemical reaction :prephenate \rightleftharpoons phenylpyruvate + H2O + CO2 This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is prephenate hydro-lyase (decarboxylating; phenylpyruvate-forming). This enzyme is also called prephenate hydro-lyase (decarboxylating). This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis. Structural studies As of late 2007, only one structure A structure is an arrangement and organization of interrelated elements in a material object or system, or the object or system so organized. Material structures include man-made objects such as buildings and machines and natural objects such as ... has been solved for this class of enzymes, with the PDB accession code . References * * * EC 4.2.1 Enzymes of known structure {{4.2-enzyme-stub ...
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Aspartate
Aspartic acid (symbol Asp or D; the ionic form is known as aspartate), is an α-amino acid that is used in the biosynthesis of proteins. The L-isomer of aspartic acid is one of the 22 proteinogenic amino acids, i.e., the building blocks of proteins. D-aspartic acid is one of two D-amino acids commonly found in mammals. Apart from a few rare exceptions, D-aspartic acid is not used for protein synthesis but is incorporated into some peptides and plays a role as a neurotransmitter/ neuromodulator. Like all other amino acids, aspartic acid contains an amino group and a carboxylic acid. Its α-amino group is in the protonated –NH form under physiological conditions, while its α-carboxylic acid group is deprotonated −COO− under physiological conditions. Aspartic acid has an acidic side chain (CH2COOH) which reacts with other amino acids, enzymes and proteins in the body. Under physiological conditions (pH 7.4) in proteins the side chain usually occurs as the negatively charged as ...
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Glutamate
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 Essential amino acid, 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 optical rotation, 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 carboxylic acid, carboxyl groups −COOH and one amine, amino group � ...
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