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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] |
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] |
Endopeptidase
Endopeptidase or endoproteinase are proteolytic peptidases that break peptide bonds of nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids. For this reason, endopeptidases cannot break down peptides into monomers, while exopeptidases can break down proteins into monomers. A particular case of endopeptidase is the oligopeptidase, whose substrates are oligopeptides instead of proteins. They are usually very specific for certain amino acids. Examples of endopeptidases include: * Trypsin - cuts after Arg or Lys, unless followed by Pro. Very strict. Works best at pH 8. * Chymotrypsin - cuts after Phe, Trp, or Tyr, unless followed by Pro. Cuts more slowly after His, Met or Leu. Works best at pH 8. * Elastase - cuts after Ala, Gly, Ser, or Val, unless followed by Pro. * Thermolysin - cuts ''before'' Ile, Met, Phe, Trp, Tyr, or Val, unless ''preceded'' by Pro. Sometimes cuts after Ala, Asp ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycine
Glycine (symbol Gly or G; ) is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid (carbamic acid is unstable), with the chemical formula NH2‐ CH2‐ COOH. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). Glycine is integral to the formation of alpha-helices in secondary protein structure due to its compact form. For the same reason, it is the most abundant amino acid in collagen triple-helices. Glycine is also an inhibitory neurotransmitter – interference with its release within the spinal cord (such as during a ''Clostridium tetani'' infection) can cause spastic paralysis due to uninhibited muscle contraction. It is the only achiral proteinogenic amino acid. It can fit into hydrophilic or hydrophobic environments, due to its minimal side chain of only one hydrogen atom. History and etymology Glycine was discovered in 1820 by the French chemist He ... [...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 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] |
