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Gingipain R
Gingipain R (, ''Arg-gingipain'', ''gingipain-1'', ''argingipain'', ''Arg-gingivain-55 proteinase'', ''Arg-gingivain-70 proteinase'', ''Arg-gingivain-75 proteinase'', ''arginine-specific cysteine protease'', ''arginine-specific gingipain'', ''arginine-specific gingivain'', ''RGP-1'', ''RGP'') is an enzyme. This enzyme catalyses the following chemical reaction: : Hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1 (position 1) This enzyme is secreted cysteine endopeptidase from the bacterium '' Porphyromonas gingivalis''. See also * Gingipain Gingipains are a family of proteases secreted by ''Porphyromonas gingivalis''. Among other functions, it works to degrade cytokines, thereby downregulating the host response in the form of reduced inflammation. Gingipain has been studied for its p ... ** Gingipain K References External links * {{Portal bar, Biology, border=no EC 3.4.22 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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] |
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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hydrolysis
Hydrolysis (; ) is any chemical reaction in which a molecule of water breaks one or more chemical bonds. The term is used broadly for substitution reaction, substitution, elimination reaction, elimination, and solvation reactions in which water is the nucleophile. Biological hydrolysis is the cleavage of biomolecules where a water molecule is consumed to effect the separation of a larger molecule into component parts. When a carbohydrate is broken into its component sugar molecules by hydrolysis (e.g., sucrose being broken down into glucose and fructose), this is recognized as saccharification. Hydrolysis reactions can be the reverse of a condensation reaction in which two molecules join into a larger one and eject a water molecule. Thus hydrolysis adds water to break down, whereas condensation builds up by removing water. Types Usually hydrolysis is a chemical process in which a molecule of water is added to a substance. Sometimes this addition causes both the substance and w ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Arginine
Arginine is the amino acid with the formula (H2N)(HN)CN(H)(CH2)3CH(NH2)CO2H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO2−) and both the amino and guanidino groups are protonated, resulting in a cation. Only the -arginine (symbol Arg or R) enantiomer is found naturally. Arg residues are common components of proteins. It is encoded by the codons CGU, CGC, CGA, CGG, AGA, and AGG. The guanidine group in arginine is the precursor for the biosynthesis of nitric oxide. Like all amino acids, it is a white, water-soluble solid. History Arginine was first isolated in 1886 from yellow lupin seedlings by the German chemist Ernst Schulze and his assistant Ernst Steiger. He named it from the Greek ''árgyros'' (ἄργυρος) meaning "silver" due to the silver-white appearance of arginine nitrate crystals. In 1897, Schulze and Ernst Winterstein (1865–1949) determined the structure ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cysteine Endopeptidase
Cysteine proteases, also known as thiol proteases, are hydrolase enzymes that degrade proteins. These proteases share a common catalysis, catalytic mechanism that involves a nucleophile, nucleophilic cysteine thiol in a catalytic triad or dyad. Discovered by Gopal Chunder Roy in 1873, the first cysteine protease to be isolated and characterized was papain, obtained from Papaya, ''Carica papaya''. Cysteine proteases are commonly encountered in fruits including the papaya, pineapple, Common fig, fig and kiwifruit. The proportion of protease tends to be higher when the fruit is unripe. In fact, the latex of dozens of different plant Family (biology), families are known to contain cysteine proteases. Cysteine proteases are used as an ingredient in meat tenderizers. Classification The MEROPS protease classification system counts 14 protein superfamily, superfamilies plus several currently unassigned families (as of 2013) each containing many protein family, families. Each superfamily ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bacterium
Bacteria (; singular: bacterium) are ubiquitous, mostly free-living organisms often consisting of one biological cell. They constitute a large domain of prokaryotic microorganisms. Typically a few micrometres in length, bacteria were among the first life forms to appear on Earth, and are present in most of its habitats. Bacteria inhabit soil, water, acidic hot springs, radioactive waste, and the deep biosphere of Earth's crust. Bacteria are vital in many stages of the nutrient cycle by recycling nutrients such as the fixation of nitrogen from the atmosphere. The nutrient cycle includes the decomposition of dead bodies; bacteria are responsible for the putrefaction stage in this process. In the biological communities surrounding hydrothermal vents and cold seeps, extremophile bacteria provide the nutrients needed to sustain life by converting dissolved compounds, such as hydrogen sulphide and methane, to energy. Bacteria also live in symbiotic and parasitic relationshi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Porphyromonas Gingivalis
''Porphyromonas gingivalis'' belongs to the phylum '' Bacteroidota'' and is a nonmotile, Gram-negative, rod-shaped, anaerobic, pathogenic bacterium. It forms black colonies on blood agar. It is found in the oral cavity, where it is implicated in periodontal disease, as well as in the upper gastrointestinal tract, the respiratory tract and the colon. It has been isolated from women with bacterial vaginosis. Collagen degradation observed in chronic periodontal disease results in part from the collagenase enzymes of this species. It has been shown in an ''in vitro'' study that ''P. gingivalis'' can invade human gingival fibroblasts and can survive in the presence of antibiotics. ''P. gingivalis'' invades gingival epithelial cells in high numbers, in which case both bacteria and epithelial cells survive for extended periods of time. High levels of specific antibodies can be detected in patients harboring ''P. gingivalis''. ''P. gingivalis'' infection has been linked to Alz ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gingipain
Gingipains are a family of proteases secreted by ''Porphyromonas gingivalis''. Among other functions, it works to degrade cytokines, thereby downregulating the host response in the form of reduced inflammation. Gingipain has been studied for its potential role in the development of Alzheimer's disease Alzheimer's disease (AD) is a neurodegeneration, neurodegenerative disease that usually starts slowly and progressively worsens. It is the cause of 60–70% of cases of dementia. The most common early symptom is difficulty in short-term me .... See also * Gingipain R * Gingipain K References {{Portal bar, Biology, border=no Proteases EC 3.4 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gingipain K
Gingipain K (, ''Lys-gingipain'', ''PrtP proteinase'') is an enzyme. This enzyme catalyses the following chemical reaction : Endopeptidase with strict specificity for lysyl bonds Activity of this enzyme is stimulated by glycine. See also * Gingipain ** Gingipain R Gingipain R (, ''Arg-gingipain'', ''gingipain-1'', ''argingipain'', ''Arg-gingivain-55 proteinase'', ''Arg-gingivain-70 proteinase'', ''Arg-gingivain-75 proteinase'', ''arginine-specific cysteine protease'', ''arginine-specific gingipain'', ''argi ... References External links * {{Portal bar, Biology, border=no EC 3.4.22 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
