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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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme Inhibitor
An enzyme inhibitor is a molecule that binds to an enzyme and blocks its activity. Enzymes are proteins that speed up chemical reactions necessary for life, in which substrate molecules are converted into products. An enzyme facilitates a specific chemical reaction by binding the substrate to its active site, a specialized area on the enzyme that accelerates the most difficult step of the reaction. An enzyme inhibitor stops ("inhibits") this process, either by binding to the enzyme's active site (thus preventing the substrate itself from binding) or by binding to another site on the enzyme such that the enzyme's catalysis of the reaction is blocked. Enzyme inhibitors may bind reversibly or irreversibly. Irreversible inhibitors form a chemical bond with the enzyme such that the enzyme is inhibited until the chemical bond is broken. By contrast, reversible inhibitors bind non-covalently and may spontaneously leave the enzyme, allowing the enzyme to resume its function. Re ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Reaction Rate
The reaction rate or rate of reaction is the speed at which a chemical reaction takes place, defined as proportional to the increase in the concentration of a product per unit time and to the decrease in the concentration of a reactant per unit time. Reaction rates can vary dramatically. For example, the oxidative rusting of iron under Earth's atmosphere is a slow reaction that can take many years, but the combustion of cellulose in a fire is a reaction that takes place in fractions of a second. For most reactions, the rate decreases as the reaction proceeds. A reaction's rate can be determined by measuring the changes in concentration over time. Chemical kinetics is the part of physical chemistry that concerns how rates of chemical reactions are measured and predicted, and how reaction-rate data can be used to deduce probable reaction mechanisms. The concepts of chemical kinetics are applied in many disciplines, such as chemical engineering, enzymology and environmental eng ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glucosidase Enzyme
Glucosidases are the glycoside hydrolase enzymes categorized under the Enzyme Commission number, EC number 3.2.1. Function Alpha-glucosidases are enzymes involved in breaking down complex carbohydrates such as starch and glycogen into their monomers. They catalyze the cleavage of individual glucosyl residues from various glycoconjugates including alpha- or beta-linked polymers of glucose. This enzyme convert complex sugars into simpler ones. Members Different sources include different members in this class. Members marked with a "#" are considered by Medical Subject Headings, MeSH to be glucosidases. Clinical significance Alpha-glucosidases are targeted by alpha-glucosidase inhibitors such as acarbose and miglitol to control diabetes mellitus type 2. See also * DNA glycosylases * Mucopolysaccharidoses References External links * {{Portal bar, Biology, border=no Hydrolases Carbohydrates EC 3.2 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Orotidine 5'-phosphate Decarboxylase
Orotidine 5'-phosphate decarboxylase (OMP decarboxylase) or orotidylate decarboxylase is an enzyme involved in pyrimidine biosynthesis. It catalyzes the decarboxylation of orotidine monophosphate (OMP) to form uridine monophosphate (UMP). The function of this enzyme is essential to the de novo biosynthesis of the pyrimidine nucleotides uridine triphosphate, cytidine triphosphate, and thymidine triphosphate. OMP decarboxylase has been a frequent target for scientific investigation because of its demonstrated extreme catalytic efficiency and its usefulness as a selection marker for yeast strain engineering. Catalysis OMP decarboxylase is known for being an extraordinarily efficient catalyst capable of accelerating the uncatalyzed reaction rate by a factor of 1017. To put this in perspective, the uncatalysed reaction which would take ''78 million years'' to convert half the reactants into products is accelerated to ''18 milliseconds'' when catalyzed by OMP decarboxyla ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Starch
Starch or amylum is a polymeric carbohydrate consisting of numerous glucose units joined by glycosidic bonds. This polysaccharide is produced by most green plants for energy storage. Worldwide, it is the most common carbohydrate in human diets, and is contained in large amounts in staple foods such as wheat, potatoes, maize (corn), rice, and cassava (manioc). Pure starch is a white, tasteless and odorless powder that is insoluble in cold water or alcohol. It consists of two types of molecules: the linear and helical amylose and the branched amylopectin. Depending on the plant, starch generally contains 20 to 25% amylose and 75 to 80% amylopectin by weight. Glycogen, the energy reserve of animals, is a more highly branched version of amylopectin. In industry, starch is often converted into sugars, for example by malting. These sugars may be fermented to produce ethanol in the manufacture of beer, whisky and biofuel. In addition, sugars produced from processed s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Meat
Meat is animal flesh that is eaten as food. Humans have hunted, farmed, and scavenged animals for meat since prehistoric times. The establishment of settlements in the Neolithic Revolution allowed the domestication of animals such as chickens, sheep, rabbits, pigs, and cattle. This eventually led to their use in meat production on an industrial scale in slaughterhouses. Meat is mainly composed of water, protein, and fat. It is edible raw but is normally eaten after it has been cooked and seasoned or processed in a variety of ways. Unprocessed meat will spoil or rot within hours or days as a result of infection with, and decomposition by, bacteria and fungi. Meat is important to the food industry, economies, and cultures around the world. There are nonetheless people who choose to not eat meat (vegetarians) or any animal products (vegans), for reasons such as taste preferences, ethics, environmental concerns, health concerns or religious dietary rules. Terminology Th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Papain
Papain, also known as papaya proteinase I, is a cysteine protease () enzyme present in papaya (''Carica papaya'') and mountain papaya (''Vasconcellea cundinamarcensis''). It is the namesake member of the papain-like protease family. It has wide ranging commercial applications in the leather, cosmetic, textiles, detergents, food and pharmaceutical industries. In the food industry, papain is used as an active ingredient in many commercial meat tenderizers. Papain family Papain belongs to a family of related proteins, known as the papain-like protease family, with a wide variety of activities, including endopeptidases, aminopeptidases, dipeptidyl peptidases and enzymes with both exo- and endopeptidase activity. Members of the papain family are widespread, found in baculoviruses, eubacteria, yeast, and practically all protozoa, plants and mammals. The proteins are typically lysosomal or secreted, and proteolytic cleavage of the propeptide is required for enzyme activation, altho ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Detergent Enzymes
Detergent enzymes are biological enzymes that are used with detergents. They catalyze the reaction between stains and the water solution, thus aiding stain removal and improving efficiency. Laundry detergent enzymes are the largest application of industrial enzymes. They can be a part of both liquid and powder detergents. History Otto Röhm introduced the use of enzymes in detergent by using trypsin extracted from the tissues of slaughtered animals. Röhm's formula, though more successful than German household cleaning methods, was considered unstable when used with alkali and bleach. In 1959, yields were improved by microbial synthesis of proteases. Properties Laundry enzymes must be able to function normally in a wide array of conditions: water temperatures ranging from 0 to 60 °C; alkaline and acidic environments; solutions with high ionic strength; and the presence of surfactants or oxidizing agents. Types The five classes of enzymes found in laundry detergent ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Antibiotics
An antibiotic is a type of antimicrobial substance active against bacteria. It is the most important type of antibacterial agent for fighting bacterial infections, and antibiotic medications are widely used in the treatment and prevention of such infections. They may either kill or inhibit the growth of bacteria. A limited number of antibiotics also possess antiprotozoal activity. Antibiotics are not effective against viruses such as the common cold or influenza; drugs which inhibit viruses are termed antiviral drugs or antivirals rather than antibiotics. Sometimes, the term ''antibiotic''—literally "opposing life", from the Greek roots ἀντι ''anti'', "against" and βίος ''bios'', "life"—is broadly used to refer to any substance used against microbes, but in the usual medical usage, antibiotics (such as penicillin) are those produced naturally (by one microorganism fighting another), whereas non-antibiotic antibacterials (such as sulfonamides and an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Denaturation (biochemistry)
In biochemistry, denaturation is a process in which proteins or nucleic acids lose the quaternary structure, tertiary structure, and secondary structure which is present in their native state, by application of some external stress or compound such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation or heat. If proteins in a living cell are denatured, this results in disruption of cell activity and possibly cell death. Protein denaturation is also a consequence of cell death. Denatured proteins can exhibit a wide range of characteristics, from conformational change and loss of solubility to aggregation due to the exposure of hydrophobic groups. The loss of solubility as a result of denaturation is called ''coagulation''. Denatured proteins lose their 3D structure and therefore cannot function. Protein folding is key to whether a globular or membrane protein can do its job correctly; ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Temperature
Temperature is a physical quantity that expresses quantitatively the perceptions of hotness and coldness. Temperature is measured with a thermometer. Thermometers are calibrated in various temperature scales that historically have relied on various reference points and thermometric substances for definition. The most common scales are the Celsius scale with the unit symbol °C (formerly called ''centigrade''), the Fahrenheit scale (°F), and the Kelvin scale (K), the latter being used predominantly for scientific purposes. The kelvin is one of the seven base units in the International System of Units (SI). Absolute zero, i.e., zero kelvin or −273.15 °C, is the lowest point in the thermodynamic temperature scale. Experimentally, it can be approached very closely but not actually reached, as recognized in the third law of thermodynamics. It would be impossible to extract energy as heat from a body at that temperature. Temperature is important in all fields of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
