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3,9-dihydroxypterocarpan 6a-monooxygenase
In enzymology, a 3,9-dihydroxypterocarpan 6a-monooxygenase () is an enzyme that catalyzes the chemical reaction :(6aR,11aR)-3,9-dihydroxypterocarpan + NADPH + H+ + O2 \rightleftharpoons (6aS,11aS)-3,6a,9-trihydroxypterocarpan + NADP+ + H2O The 4 substrates of this enzyme are (6aR,11aR)-3,9-dihydroxypterocarpan, NADPH, H+, and O2, whereas its 3 products are (6aS,11aS)-3,6a,9-trihydroxypterocarpan, NADP+, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (6aR,11aR)-3,9-dihydroxypterocarpan,NADPH:oxygen oxidoreductase (6a-hydroxylating). Other names in common use include 3,9-dihydroxypterocarpan 6a-hydroxylase, and 3,9-dihydroxypterocarpan 6alpha-monooxygenase (erroneous). ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Water
Water (chemical formula ) is an inorganic, transparent, tasteless, odorless, and nearly colorless chemical substance, which is the main constituent of Earth's hydrosphere and the fluids of all known living organisms (in which it acts as a solvent). It is vital for all known forms of life, despite not providing food, energy or organic micronutrients. Its chemical formula, H2O, indicates that each of its molecules contains one oxygen and two hydrogen atoms, connected by covalent bonds. The hydrogen atoms are attached to the oxygen atom at an angle of 104.45°. "Water" is also the name of the liquid state of H2O at standard temperature and pressure. A number of natural states of water exist. It forms precipitation in the form of rain and aerosols in the form of fog. Clouds consist of suspended droplets of water and ice, its solid state. When finely divided, crystalline ice may precipitate in the form of snow. The gaseous state of water is steam or water vapor. Water co ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heme Enzymes
Heme, or haem (pronounced / hi:m/ ), is a precursor to hemoglobin, which is necessary to bind oxygen in the bloodstream. Heme is biosynthesized in both the bone marrow and the liver. In biochemical terms, heme is a coordination complex "consisting of an iron ion coordinated to a porphyrin acting as a tetradentate ligand, and to one or two axial ligands." The definition is loose, and many depictions omit the axial ligands. Among the metalloporphyrins deployed by metalloproteins as prosthetic groups, heme is one of the most widely used and defines a family of proteins known as hemoproteins. Hemes are most commonly recognized as components of hemoglobin, the red pigment in blood, but are also found in a number of other biologically important hemoproteins such as myoglobin, cytochromes, catalases, heme peroxidase, and endothelial nitric oxide synthase. The word ''haem'' is derived from Greek ''haima'' meaning "blood". Function Hemoproteins have diverse biological functions incl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heme
Heme, or haem (pronounced / hi:m/ ), is a precursor to hemoglobin, which is necessary to bind oxygen in the bloodstream. Heme is biosynthesized in both the bone marrow and the liver. In biochemical terms, heme is a coordination complex "consisting of an iron ion coordinated to a porphyrin acting as a tetradentate ligand, and to one or two axial ligands." The definition is loose, and many depictions omit the axial ligands. Among the metalloporphyrins deployed by metalloproteins as prosthetic groups, heme is one of the most widely used and defines a family of proteins known as hemoproteins. Hemes are most commonly recognized as components of hemoglobin, the red pigment in blood, but are also found in a number of other biologically important hemoproteins such as myoglobin, cytochromes, catalases, heme peroxidase, and endothelial nitric oxide synthase. The word ''haem'' is derived from Greek ''haima'' meaning "blood". Function Hemoproteins have diverse biological functions incl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cofactor (biochemistry)
A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction). Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound. Cofactors can be divided into two types: inorganic ions and complex organic molecules called coenzymes. Coenzymes are mostly derived from vitamins and other organic essential nutrients in small amounts. (Note that some scientists limit the use of the term "cofactor" for inorganic substances; both types are included here.) Coenzymes are further divided into two types. The first is called a "prosthetic group", which consists of a coenzyme that is tightly (or even covalently) and permanently bound to a protein. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Isoflavonoid Biosynthesis
The biosynthesis of isoflavonoids involves several enzymes; These are: Liquiritigenin,NADPH:oxygen oxidoreductase (hydroxylating, aryl migration), also known as Isoflavonoid synthase, is an enzyme that uses liquiritigenin (a flavanone), O2, NADPH and H+ to produce 2,7,4'-trihydroxyisoflavanone (an isoflavonoid), H2O and NADP+. * Biochanin-A reductase * Flavone synthase * 2'-hydroxydaidzein reductase * 2-hydroxyisoflavanone dehydratase * 2-hydroxyisoflavanone synthase * Isoflavone 4'-O-methyltransferase * Isoflavone 7-O-methyltransferase * Isoflavone 2'-hydroxylase * Isoflavone 3'-hydroxylase * Isoflavone-7-O-beta-glucoside 6"-O-malonyltransferase * Isoflavone 7-O-glucosyltransferase * 4'-methoxyisoflavone 2'-hydroxylase Pterocarpans biosynthesis * 3,9-dihydroxypterocarpan 6a-monooxygenase * Glyceollin synthase * Pterocarpin synthase See also * Flavonoid biosynthesis Flavonoids are synthesized by the phenylpropanoid metabolic pathway in which the amino acid phenylal ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
List Of Enzymes
This article lists enzymes by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission (EC) numbering system. * List of EC numbers (EC 5) * List of EC numbers (EC 6) :Oxidoreductases (EC 1) (Oxidoreductase) *Dehydrogenase * Luciferase *DMSO reductase :EC 1.1 (act on the CH-OH group of donors) * :EC 1.1.1 (with NAD+ or NADP+ as acceptor) ** Alcohol dehydrogenase (NAD) ** Alcohol dehydrogenase (NADP) **Homoserine dehydrogenase ** Aminopropanol oxidoreductase **Diacetyl reductase **Glycerol dehydrogenase **Propanediol-phosphate dehydrogenase ** glycerol-3-phosphate dehydrogenase (NAD+) ** D-xylulose reductase **L-xylulose reductase **Lactate dehydrogenase **Malate dehydrogenase **Isocitrate dehydrogenase ** HMG-CoA reductase * :EC 1.1.2 (with a cytochrome as acceptor) * :EC 1.1.3 (with oxygen as acceptor) **Glucose oxidase **L-gulonolactone oxidase **Thiamine oxidase **Xanthine oxidase * :EC 1.1.4 (with a disul ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Oxidoreductase
In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP+ or NAD+ as cofactors. Transmembrane oxidoreductases create electron transport chains in bacteria, chloroplasts and mitochondria, including respiratory complexes I, II and III. Some others can associate with biological membranes as peripheral membrane proteins or be anchored to the membranes through a single transmembrane helix. in ...
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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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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