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PFK
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 shown it com ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycolysis
Glycolysis is the metabolic pathway that converts glucose () into pyruvate (). The free energy released in this process is used to form the high-energy molecules adenosine triphosphate (ATP) and reduced nicotinamide adenine dinucleotide (NADH). Glycolysis is a sequence of ten reactions catalyzed by enzymes. Glycolysis is a metabolic pathway that does not require oxygen (In anaerobic conditions pyruvate is converted to lactic acid). The wide occurrence of glycolysis in other species indicates that it is an ancient metabolic pathway. Indeed, the reactions that make up glycolysis and its parallel pathway, the pentose phosphate pathway, occur in the oxygen-free conditions of the Archean oceans, also in the absence of enzymes, catalyzed by metal. In most organisms, glycolysis occurs in the liquid part of cells, the cytosol. The most common type of glycolysis is the ''Embden–Meyerhof–Parnas (EMP) pathway'', which was discovered by Gustav Embden, Otto Meyerhof, and Jak ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycolytic Pathway
Glycolysis is the metabolic pathway that converts glucose () into pyruvate (). The free energy released in this process is used to form the high-energy molecules adenosine triphosphate (ATP) and reduced nicotinamide adenine dinucleotide (NADH). Glycolysis is a sequence of ten reactions catalyzed by enzymes. Glycolysis is a metabolic pathway that does not require oxygen (In anaerobic conditions pyruvate is converted to lactic acid). The wide occurrence of glycolysis in other species indicates that it is an ancient metabolic pathway. Indeed, the reactions that make up glycolysis and its parallel pathway, the pentose phosphate pathway, occur in the Great Oxygenation Event, oxygen-free conditions of the Archean oceans, also in the absence of enzymes, catalyzed by metal. In most organisms, glycolysis occurs in the liquid part of cells, the cytosol. The most common type of glycolysis is the ''Embden–Meyerhof–Parnas (EMP) pathway'', which was discovered by Gustav Embden, Otto Mey ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Adenosine Triphosphate
Adenosine triphosphate (ATP) is an organic compound that provides energy to drive many processes in living cells, such as muscle contraction, nerve impulse propagation, condensate dissolution, and chemical synthesis. Found in all known forms of life, ATP is often referred to as the "molecular unit of currency" of intracellular energy transfer. When consumed in metabolic processes, it converts either to adenosine diphosphate (ADP) or to adenosine monophosphate (AMP). Other processes regenerate ATP. The human body recycles its own body weight equivalent in ATP each day. It is also a precursor to DNA and RNA, and is used as a coenzyme. From the perspective of biochemistry, ATP is classified as a nucleoside triphosphate, which indicates that it consists of three components: a nitrogenous base ( adenine), the sugar ribose, and the triphosphate. Structure ATP consists of an adenine attached by the 9-nitrogen atom to the 1′ carbon atom of a sugar ( ribose), which in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Kinase
In biochemistry, a kinase () is an enzyme that catalysis, catalyzes the transfer of phosphate groups from High-energy phosphate, high-energy, phosphate-donating molecules to specific Substrate (biochemistry), substrates. This process is known as phosphorylation, where the high-energy adenosine triphosphate, ATP molecule donates a phosphate group to the substrate (biology), substrate molecule. This transesterification produces a phosphorylated substrate and Adenosine diphosphate, ADP. Conversely, it is referred to as dephosphorylation when the phosphorylated substrate donates a phosphate group and adenosine diphosphate, ADP gains a phosphate group (producing a dephosphorylated substrate and the high energy molecule of ATP). These two processes, phosphorylation and dephosphorylation, occur four times during glycolysis. Kinases are part of the larger family of phosphotransferases. Kinases should not be confused with phosphorylases, which catalyze the addition of inorganic phosphate ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Allosteric Regulation
In biochemistry, allosteric regulation (or allosteric control) is the regulation of an enzyme by binding an effector molecule at a site other than the enzyme's active site. The site to which the effector binds is termed the ''allosteric site'' or ''regulatory site''. Allosteric sites allow effectors to bind to the protein, often resulting in a conformational change and/or a change in protein dynamics. Effectors that enhance the protein's activity are referred to as ''allosteric activators'', whereas those that decrease the protein's activity are called ''allosteric inhibitors''. Allosteric regulations are a natural example of control loops, such as feedback from downstream products or feedforward from upstream substrates. Long-range allostery is especially important in cell signaling. Allosteric regulation is also particularly important in the cell's ability to adjust enzyme activity. The term ''allostery'' comes from the Ancient Greek ''allos'' (), "other", and ''stereos' ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ribokinase
In enzymology, a ribokinase () is an enzyme that catalyzes the chemical reaction :ATP + -ribose ⇌ ADP + -ribose 5-phosphate Thus, the two substrates of this enzyme are ATP and -ribose, whereas its two products are ADP and -ribose 5-phosphate. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivial ... of this enzyme class is ATP:-ribose 5-phosphotransferase. Other names in common use include deoxyribokinase, ribokinase (phosphorylating), and -ribokinase. This enzyme participates in pentose phosphate pathway. Ribokinase (RK) belongs to the phosphofructokinase B (PfkB) family of sugar kinases. Other members of this family (also known as the RK family) include adenosine kinase (AK), inosine-guanosine kinase, fructokinase, and 1-phosphofructokinase. The members o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Adenosine Kinase
Adenosine kinase (AdK; EC 2.7.1.20) is an enzyme that catalyzes the transfer of gamma-phosphate from Adenosine triphosphate (ATP) to adenosine Adenosine (symbol A) is an organic compound that occurs widely in nature in the form of diverse derivatives. The molecule consists of an adenine attached to a ribose via a β-N9-glycosidic bond. Adenosine is one of the four nucleoside buildin ... (Ado) leading to formation of Adenosine monophosphate ( AMP). In addition to its well-studied role in controlling the cellular concentration of Ado, AdK also plays an important role in the maintenance of methylation reactions. All S-adenosylmethionine-dependent transmethylation reactions in cells lead to production of S-adenosylhomocysteine (SAH), which is cleaved by SAH hydrolase into Ado and homocysteine. The failure to efficiently remove these end products (Ado removed by phosphorylation by AdK) can result in buildup of SAH, which is a potent inhibitor of all transmethylation reactions. The ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Inosine Kinase
In enzymology, an inosine kinase () is an enzyme that catalyzes the chemical reaction :ATP + inosine \rightleftharpoons ADP + IMP Thus, the two substrates of this enzyme are ATP and inosine, whereas its two products are ADP and IMP. Inosine kinase belongs to the phosphofructokinase B (PfkB) family of sugar kinases.Park J, Gupta RS: Adenosine kinase and ribokinase--the RK family of proteins. Cell Mol Life Sci 2008, 65: 2875-2896. Other members of this family (also known as the Ribokinase family) include ribokinase (RK) adenosine kinase (AK), fructokinase, and 1-phosphofructokinase.Bork P, Sander C, Valencia A: Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases. Protein Sci 1993, 2: 31-40.Spychala J, Datta NS, Takabayashi K, Datta M, Fox IH, Gribbin T, Mitchell BS: Cloning of human adenosine kinase cDNA: sequence similarity to microbial ribokinases and fructokinases. Proc Natl Ac ... [...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 st ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Reaction Mechanism
In chemistry, a reaction mechanism is the step by step sequence of elementary reactions by which overall chemical change occurs. A chemical mechanism is a theoretical conjecture that tries to describe in detail what takes place at each stage of an overall chemical reaction. The detailed steps of a reaction are not observable in most cases. The conjectured mechanism is chosen because it is thermodynamically feasible, and has experimental support in isolated intermediates (see next section) or other quantitative and qualitative characteristics of the reaction. It also describes each reactive intermediate, activated complex, and transition state, and which bonds are broken (and in what order), and which bonds are formed (and in what order). A complete mechanism must also explain the reason for the reactants and catalyst used, the stereochemistry observed in reactants and products, all products formed and the amount of each. The electron or arrow pushing method is often used ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
