2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline Decarboxylase
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2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline Decarboxylase
In molecular biology 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (OHCU decarboxylase) is an enzyme involved in purine catabolism. It catalyses the decarboxylation Decarboxylation is a chemical reaction that removes a carboxyl group and releases carbon dioxide (CO2). Usually, decarboxylation refers to a reaction of carboxylic acids, removing a carbon atom from a carbon chain. The reverse process, which is t ... of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) into S(+)-allantoin. It is the third step of the conversion of uric acid (a purine derivative) to allantoin. Step one is catalysed by urate oxidase and step two is catalysed by hydroxyisourate hydrolase. References {{InterPro content, IPR018020 Protein domains ...
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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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Purine
Purine is a heterocyclic compound, heterocyclic aromatic organic compound that consists of two rings (pyrimidine and imidazole) fused together. It is water-soluble. Purine also gives its name to the wider class of molecules, purines, which include substituted purines and their tautomers. They are the most widely occurring nitrogen-containing heterocycles in nature. Dietary sources Purines are found in high concentration in meat and meat products, especially internal organs such as liver and kidney. In general, plant-based diets are low in purines. High-purine plants and algae include some legumes (lentils and Black-eyed pea, black eye peas) and Spirulina (dietary supplement), spirulina. Examples of high-purine sources include: sweetbreads, Anchovies as food, anchovies, Sardines as food, sardines, liver, beef kidneys, Brain as food, brains, meat extracts (e.g., Oxo (food), Oxo, Bovril), herring, mackerel, scallops, game meats, yeast (beer, yeast extract, nutritional yeast) and g ...
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Catabolism
Catabolism () is the set of metabolic pathways that breaks down molecules into smaller units that are either oxidized to release energy or used in other anabolic reactions. Catabolism breaks down large molecules (such as polysaccharides, lipids, nucleic acids, and proteins) into smaller units (such as monosaccharides, fatty acids, nucleotides, and amino acids, respectively). Catabolism is the breaking-down aspect of metabolism, whereas anabolism is the building-up aspect. Cells use the monomers released from breaking down polymers to either construct new polymer molecules or degrade the monomers further to simple waste products, releasing energy. Cellular wastes include lactic acid, acetic acid, carbon dioxide, ammonia, and urea. The formation of these wastes is usually an oxidation process involving a release of chemical free energy, some of which is lost as heat, but the rest of which is used to drive the synthesis of adenosine triphosphate (ATP). This molecule acts as a way f ...
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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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Decarboxylation
Decarboxylation is a chemical reaction that removes a carboxyl group and releases carbon dioxide (CO2). Usually, decarboxylation refers to a reaction of carboxylic acids, removing a carbon atom from a carbon chain. The reverse process, which is the first chemical step in photosynthesis, is called carboxylation, the addition of CO2 to a compound. Enzymes that catalyze decarboxylations are called decarboxylases or, the more formal term, carboxy-lyases (Enzyme Commission number, EC number 4.1.1). In organic chemistry The term "decarboxylation" usually means replacement of a carboxyl group () with a hydrogen atom: :RCO2H -> RH + CO2 Decarboxylation is one of the oldest known organic reactions. It is one of the processes assumed to accompany pyrolysis and destructive distillation. Metal salts, especially copper compounds, facilitate the reaction via the intermediacy of metal carboxylate complexes. Decarboxylation of aryl carboxylates can generate the equivalent of the correspond ...
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Urate Oxidase
The enzyme urate oxidase (UO), uricase or factor-independent urate hydroxylase, absent in humans, catalyzes the oxidation of uric acid to 5-hydroxyisourate: :Uric acid + O2 + H2O → 5-hydroxyisourate + H2O2 : 5-hydroxyisourate + H2O → allantoin + CO2 Image:Uric acid.png, Uric acid Image:5-Hydroxyisourate.svg, 5-Hydroxyisourate Image:Allantoin.svg, Allantoin Structure Urate oxidase is mainly localised in the liver, where it forms a large electron-dense paracrystalline core in many peroxisomes. The enzyme exists as a tetramer of identical subunits, each containing a possible type 2 copper-binding site. Urate oxidase is a homotetrameric enzyme containing four identical active sites situated at the interfaces between its four subunits. UO from '' A. flavus'' is made up of 301 residues and has a molecular weight of 33438 daltons. It is unique among the oxidases in that it does not require a metal atom or an organic co-factor for catalysis. Sequence analysis of severa ...
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Hydroxyisourate Hydrolase
In enzymology, a hydroxyisourate hydrolase () is an enzyme that catalyzes the chemical reaction :5-hydroxyisourate + H2O \rightleftharpoons 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate Thus, the two substrates of this enzyme are 5-hydroxyisourate and H2O, whereas its product is 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is 5-hydroxyisourate amidohydrolase. Other names in common use include HIUHase, and 5-hydroxyisourate hydrolase. This enzyme participates in purine metabolism. Structural studies As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and . See also *2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase In molecular biology 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decar ...
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