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Enzyme Memory
Enzyme memory is a concept in enzyme kinetics based on the idea that the kinetic properties of an enzyme may vary according to conditions in its previous catalytic cycle. It can occur both in ternary-complex mechanisms and in substituted-enzyme Enzyme kinetics#Multi-substrate reactions, ("ping-pong") mechanisms, with very different consequences. Ternary-complex mechanism A mnemonical mechanism for a reaction A + B → products that proceeds through a ternary complex EAB is shown in the illustration at the right. The essential characteristic, that makes this different from any mechanism in which substrate binding is at or close to equilibrium, is that it contains both slow and fast steps, with the fast step preventing the binding from reaching equilibrium, because release of products is too rapid to allow this. The enzyme exists in two forms: as a free enzyme it exists as E′, but the form released at the end of the catalytic cycle is E. E′ is the form that exists during the c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme Kinetics
Enzyme kinetics is the study of the rates of enzyme catalysis, enzyme-catalysed chemical reactions. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated. Studying an enzyme's chemical kinetics, kinetics in this way can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or a modifier (Enzyme inhibitor, inhibitor or Enzyme activator, activator) might affect the rate. An enzyme (E) is a protein molecule that serves as a biological catalyst to facilitate and accelerate a chemical reaction in the body. It does this through binding of another molecule, its Substrate (biochemistry), substrate (S), which the enzyme acts upon to form the desired product. The substrate binds to the active site of the enzyme to produce an enzyme-substrate complex ES, and is transformed into an enzyme-product complex EP and from there to product P, via a transition state ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phosphofructokinase
Phosphofructokinase (PFK) is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis. Function The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes. Phosphofructokinase catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the glycolytic pathway. It is allosterically inhibited by ATP and allosterically activated by AMP, thus indicating the cell's energetic needs when it undergoes the glycolytic pathway. PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha- (PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian monomers, possessing 2 similar domains). This protein may use the morpheein model of allosteric regulation. PFK is about 300 amino acids in length, and structural studies of the bacterial enzyme have show ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Rhodanese
Rhodanese is a mitochondrial enzyme that detoxifies cyanide (CN−) by converting it to thiocyanate (SCN−, also known as "rhodanate"). In enzymatology, the common name is listed as thiosulfate sulfurtransferase (). The diagram on the right shows the crystallographically-determined structure of rhodanese. It catalyzes the following reaction: :thiosulfate + cyanide \rightleftharpoons sulfite + thiocyanate Structure and mechanism This reaction takes place in two steps. In the first step, thiosulfate is reduced by the thiol group on cysteine-247 1, to form a persulfide and a sulfite 2. In the second step, the persulfide reacts with cyanide to produce thiocyanate, re-generating the cysteine thiol 1. Rhodanese shares evolutionary relationship with a large family of proteins, including: * Cdc25 phosphatase catalytic domain * non-catalytic domains of eukaryotic dual-specificity MAPK-phosphatases * non-catalytic domains of yeast PTP-type MAPK-phosphatases * non-catalytic doma ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ascorbate Oxidase
Vitamin C (also known as ascorbic acid and ascorbate) is a water-soluble vitamin found in citrus and other fruits, berries and vegetables. It is also a generic prescription medication and in some countries is sold as a non-prescription dietary supplement. As a therapy, it is used to prevent and treat scurvy, a disease caused by vitamin C deficiency. Vitamin C is an essential nutrient involved in the repair of tissue, the formation of collagen, and the enzymatic production of certain neurotransmitters. It is required for the functioning of several enzymes and is important for immune system function. It also functions as an antioxidant. Vitamin C may be taken by mouth or by intramuscular, subcutaneous or intravenous injection. Various health claims exist on the basis that moderate vitamin C deficiency increases disease risk, such as for the common cold, cancer or COVID-19. There are also claims of benefits from vitamin C supplementation in excess of the recommended dietary ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aspartate Aminotransferase
Aspartate transaminase (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or (serum) glutamic oxaloacetic transaminase (GOT, SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme () that was first described by Arthur Karmen and colleagues in 1954. AST catalyzes the reversible transfer of an α-amino group between aspartate and glutamate and, as such, is an important enzyme in amino acid metabolism. AST is found in the liver, heart, skeletal muscle, kidneys, brain, red blood cells and gall bladder. Serum AST level, serum ALT (alanine transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood test, blood panels. The biological half-life, half-life of total AST in the circulation approximates 17 hours and, on average, 87 hours for ''mitochondrial'' AST. Aminotransferase is cleared by Liver sinusoidal endothelial cell, sinusoidal cells in the liver. Function Aspartate ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
John Westley (biochemist)
John W. Westley (1927–) was an enzymologist at the University of Chicago The University of Chicago (UChicago, Chicago, or UChi) is a Private university, private research university in Chicago, Illinois, United States. Its main campus is in the Hyde Park, Chicago, Hyde Park neighborhood on Chicago's South Side, Chic ..., best known for his research on rhodanese and other sulfurtransferases. Education and employment John Westley obtained his Ph.D. in 1954 at the University of Chicago on the basis of a thesis entitled "Studies on the synthesis of histidine by ''Escherichia coli''". He subsequently worked in the Department of Biochemistry (now Department of Biochemistry & Molecular Biology) of the University of Chicago. Research John Westley's doctoral research concerned the biosynthesis of histidine in ''Escherichia coli''. Subsequently he became an enzymologist and worked principally on rhodanese (thiosulfate sulfurtransferase, EC 2.8.1.1), starting with a comparison o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nitrate Reductase
Nitrate reductases are molybdoenzymes that reduce nitrate () to nitrite (). This reaction is critical for the production of protein in most crop plants, as nitrate is the predominant source of nitrogen in fertilized soils. Types Eukaryotic Eukaryotic nitrate reductases are part of the sulfite oxidase family of molybdoenzymes. They transfer electrons from NADH or NADPH to nitrate. Prokaryotic Prokaryotic nitrate reductases belong to the DMSO reductase family of molybdoenzymes and have been classified into three groups, assimilatory nitrate reductases (Nas), respiratory nitrate reductase (Nar), and periplasmic nitrate reductases (Nap). The active site of these enzymes is a molybdenum ion that is bound to the four thiolate functional groups of two pterin molecules. The coordination sphere of the molybdenum ion is completed by one amino-acid side chain and oxygen and/or sulfur ligands. In Nap, the molybdenum is covalently attached to the protein by a cysteine side cha ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
