Catechol 1,2-dioxygenase
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Catechol 1,2-dioxygenase
Catechol 1,2- dioxygenase (, ''1,2-CTD'', ''catechol-oxygen 1,2-oxidoreductase'', ''1,2-pyrocatechase'', ''catechase'', ''catechol 1,2-oxygenase'', '' catechol dioxygenase'', ''pyrocatechase'', ''pyrocatechol 1,2-dioxygenase'', ''CD I'', ''CD II'') is an enzyme that catalyzes the oxidative ring cleavage of catechol to form ''cis,cis''-muconic acid: More specifically, 1,2-CTD is an intradiol dioxygenase, a family of catechol dioxygenases that cleaves the bond between the phenolic hydroxyl groups of catechol using an Fe3+ cofactor. Thus far, 1,2-CTD has been observed to exist in the following species of soil bacteria and fungi: '' Pseudomonas sp.'', ''Pseudomonas fluorescens'', '' Aspergillus niger'', ''Brevibacterium fuscum'', '' Acinetobacter calcoaceticus'', '' Trichosporon cutaneum'', '' Rhodococcus erythropolis'', ''Frateuria sp.'', ''Rhizobium trifolii'', '' Pseudomonas putida'', ''Candida tropicalis'', ''Candida maltose'', ''Rhizobium leguminosarum'', and '' Nocardia s ...
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Catechol Dioxygenase
Catechol dioxygenases are metalloprotein enzymes that carry out the oxidative cleavage of catechols. This class of enzymes incorporate dioxygen into the substrate. Catechol dioxygenases belong to the class of oxidoreductases and have several different substrate specificities, including catechol 1,2-dioxygenase (), catechol 2,3-dioxygenase (), and protocatechuate 3,4-dioxygenase (). The active site of catechol dioxygenases most frequently contains iron, but manganese-containing forms are also known. The ''Pseudomonas putida'' xylE gene, which encodes catechol 2,3-dioxygenase, is often used as a reporter to quantitate gene expression. An example of the reaction carried out by catechol 1,2-dioxygenase is the formation of ''cis,cis''-muconic acid from catechol, shown below. See also * Bioinorganic chemistry * Oxygenase An oxygenase is any enzyme that oxidizes a substrate by transferring the oxygen from molecular oxygen O2 (as in air) to it. The oxygenases form a class of oxi ...
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Rhizobium
''Rhizobium'' is a genus of Gram-negative soil bacteria that fix nitrogen. ''Rhizobium'' species form an endosymbiotic nitrogen-fixing association with roots of (primarily) legumes and other flowering plants. The bacteria colonize plant cells within root nodules, where they convert atmospheric nitrogen into ammonia using the enzyme nitrogenase and then provide organic nitrogenous compounds such as glutamine or ureides to the plant. The plant, in turn, provides the bacteria with organic compounds made by photosynthesis. This mutually beneficial relationship is true of all of the rhizobia, of which the genus ''Rhizobium'' is a typical example. ''Rhizobium'' is also capable to solubilize phosphorus. History Martinus Beijerinck was the first to isolate and cultivate a microorganism from the nodules of legumes in 1888. He named it ''Bacillus radicicola'', which is now placed in ''Bergey's Manual of Determinative Bacteriology'' under the genus ''Rhizobium''. Research ''Rhizobium'' ...
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Crystallography
Crystallography is the experimental science of determining the arrangement of atoms in crystalline solids. Crystallography is a fundamental subject in the fields of materials science and solid-state physics (condensed matter physics). The word "crystallography" is derived from the Greek word κρύσταλλος (''krystallos'') "clear ice, rock-crystal", with its meaning extending to all solids with some degree of transparency, and γράφειν (''graphein'') "to write". In July 2012, the United Nations recognised the importance of the science of crystallography by proclaiming that 2014 would be the International Year of Crystallography. denote a direction vector (in real space). * Coordinates in ''angle brackets'' or ''chevrons'' such as <100> denote a ''family'' of directions which are related by symmetry operations. In the cubic crystal system for example, would mean 00 10 01/nowiki> or the negative of any of those directions. * Miller indices in ''parentheses'' ...
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Catechol 1,2-dioxygenase Mechanism
Catechol ( or ), also known as pyrocatechol or 1,2-dihydroxybenzene, is a toxic organic compound with the molecular formula . It is the ''ortho'' isomer of the three isomeric benzenediols. This colorless compound occurs naturally in trace amounts. It was first discovered by destructive distillation of the plant extract catechin. About 20,000 tonnes of catechol are now synthetically produced annually as a commodity organic chemical, mainly as a precursor to pesticides, flavors, and fragrances. Catechol occurs as feathery white crystals that are very rapidly soluble in water. Isolation and synthesis Catechol was first isolated in 1839 by Edgar Hugo Emil Reinsch (1809–1884) by distilling it from the solid tannic preparation catechin, which is the residuum of catechu, the boiled or concentrated juice of ''Mimosa catechu'' ('' Acacia catechu''). Upon heating catechin above its decomposition point, a substance that Reinsch first named ''Brenz-Katechusäure'' (burned catechu a ...
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Alpha Helix
The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a right hand-helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid located four residues earlier along the protein sequence. The alpha helix is also called a classic Pauling–Corey–Branson α-helix. The name 3.613-helix is also used for this type of helix, denoting the average number of residues per helical turn, with 13 atoms being involved in the ring formed by the hydrogen bond. Among types of local structure in proteins, the α-helix is the most extreme and the most predictable from sequence, as well as the most prevalent. Discovery In the early 1930s, William Astbury showed that there were drastic changes in the X-ray fiber diffraction of moist wool or hair fibers upon significant stretching. The data suggested that the unstretched fibers had a coiled molecular structure with a characteristic repeat of ≈. Astb ...
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Trigonal Bipyramidal Molecular Geometry
In chemistry, a trigonal bipyramid formation is a molecular geometry with one atom at the center and 5 more atoms at the corners of a triangular bipyramid. This is one geometry for which the bond angles surrounding the central atom are not identical (see also pentagonal bipyramid), because there is no geometrical arrangement with five terminal atoms in equivalent positions. Examples of this molecular geometry are phosphorus pentafluoride (), and phosphorus pentachloride () in the gas phase. Axial (or apical) and equatorial positions The five atoms bonded to the central atom are not all equivalent, and two different types of position are defined. For phosphorus pentachloride as an example, the phosphorus atom shares a plane with three chlorine atoms at 120° angles to each other in ''equatorial'' positions, and two more chlorine atoms above and below the plane (''axial'' or ''apical'' positions). According to the VSEPR theory of molecular geometry, an axial position is more crowd ...
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Coordination Complex
A coordination complex consists of a central atom or ion, which is usually metallic and is called the ''coordination centre'', and a surrounding array of bound molecules or ions, that are in turn known as ''ligands'' or complexing agents. Many metal-containing compounds, especially those that include transition metals (elements like titanium that belong to the Periodic Table's d-block), are coordination complexes. Nomenclature and terminology Coordination complexes are so pervasive that their structures and reactions are described in many ways, sometimes confusingly. The atom within a ligand that is bonded to the central metal atom or ion is called the donor atom. In a typical complex, a metal ion is bonded to several donor atoms, which can be the same or different. A polydentate (multiple bonded) ligand is a molecule or ion that bonds to the central atom through several of the ligand's atoms; ligands with 2, 3, 4 or even 6 bonds to the central atom are common. These compl ...
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Random Coil
In polymer chemistry, a random coil is a conformation of polymers where the monomer subunits are oriented randomly while still being bonded to adjacent units. It is not one specific shape, but a statistical distribution of shapes for all the chains in a population of macromolecules. The conformation's name is derived from the idea that, in the absence of specific, stabilizing interactions, a polymer backbone will "sample" all possible conformations randomly. Many unbranched, linear homopolymers — in solution, or above their melting temperatures — assume (approximate) random coils. Random walk model: The Gaussian chain There are an enormous number of different ways in which a chain can be curled around in a relatively compact shape, like an unraveling ball of twine with much open space, and comparatively few ways it can be more or less stretched out. So, if each conformation has an equal probability or statistical weight, chains are much more likely to be ball-like than ...
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Beta Sheet
The beta sheet, (β-sheet) (also β-pleated sheet) is a common motif of the regular protein secondary structure. Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation. The supramolecular association of β-sheets has been implicated in the formation of the fibrils and protein aggregates observed in amyloidosis, notably Alzheimer's disease. History The first β-sheet structure was proposed by William Astbury in the 1930s. He proposed the idea of hydrogen bonding between the peptide bonds of parallel or antiparallel extended β-strands. However, Astbury did not have the necessary data on the bond geometry of the amino acids in order to build accurate models, especially since he did not then know that the peptide bond was planar. A refined versi ...
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Protein Dimer
In biochemistry, a protein dimer is a macromolecular complex formed by two protein monomers, or single proteins, which are usually non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word ''dimer'' has roots meaning "two parts", '' di-'' + '' -mer''. A protein dimer is a type of protein quaternary structure. A protein homodimer is formed by two identical proteins. A protein heterodimer is formed by two different proteins. Most protein dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is composed of two different amino acid chains. An exception is dimers that are linked by disulfide bridges such as the homodimeric protein NEMO. Some proteins contain specialized domains to ensure dimerization (dimerization domains) and specificity. The G protein-coupled cannabinoid receptors have the ability to form both homo- and heterodimers with several ...
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Catechol 1,2-dioxygenase
Catechol 1,2- dioxygenase (, ''1,2-CTD'', ''catechol-oxygen 1,2-oxidoreductase'', ''1,2-pyrocatechase'', ''catechase'', ''catechol 1,2-oxygenase'', '' catechol dioxygenase'', ''pyrocatechase'', ''pyrocatechol 1,2-dioxygenase'', ''CD I'', ''CD II'') is an enzyme that catalyzes the oxidative ring cleavage of catechol to form ''cis,cis''-muconic acid: More specifically, 1,2-CTD is an intradiol dioxygenase, a family of catechol dioxygenases that cleaves the bond between the phenolic hydroxyl groups of catechol using an Fe3+ cofactor. Thus far, 1,2-CTD has been observed to exist in the following species of soil bacteria and fungi: '' Pseudomonas sp.'', ''Pseudomonas fluorescens'', '' Aspergillus niger'', ''Brevibacterium fuscum'', '' Acinetobacter calcoaceticus'', '' Trichosporon cutaneum'', '' Rhodococcus erythropolis'', ''Frateuria sp.'', ''Rhizobium trifolii'', '' Pseudomonas putida'', ''Candida tropicalis'', ''Candida maltose'', ''Rhizobium leguminosarum'', and '' Nocardia s ...
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