2-oxoglutarate Dehydrogenase
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2-oxoglutarate Dehydrogenase
The oxoglutarate dehydrogenase complex (OGDC) or α-ketoglutarate dehydrogenase complex is an enzyme complex, most commonly known for its role in the citric acid cycle. Units Much like pyruvate dehydrogenase complex (PDC), this enzyme forms a complex composed of three components: Three classes of these multienzyme complexes have been characterized: one specific for pyruvate, a second specific for 2-oxoglutarate, and a third specific for branched-chain amino acid, branched-chain α-keto acids. The oxoglutarate dehydrogenase complex has the same subunit structure and thus uses the same coenzymes as the pyruvate dehydrogenase complex and the branched-chain alpha-keto acid dehydrogenase complex (TTP, CoA, lipoate, FAD and NAD). Only the E3 subunit is shared in common between the three enzymes. Properties Metabolic pathways This enzyme participates in three different pathways: * Citric acid cycle (KEGG linkMAP00020 * Lysine degradation (KEGG linkMAP00310 * Tryptophan metabolism ...
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Citric Acid Cycle
The citric acid cycle (CAC)—also known as the Krebs cycle or the TCA cycle (tricarboxylic acid cycle)—is a series of chemical reactions to release stored energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins. The Krebs cycle is used by organisms that respire (as opposed to organisms that ferment) to generate energy, either by anaerobic respiration or aerobic respiration. In addition, the cycle provides precursors of certain amino acids, as well as the reducing agent NADH, that are used in numerous other reactions. Its central importance to many biochemical pathways suggests that it was one of the earliest components of metabolism and may have originated abiogenically. Even though it is branded as a 'cycle', it is not necessary for metabolites to follow only one specific route; at least three alternative segments of the citric acid cycle have been recognized. The name of this metabolic pathway is derived from the citric acid (a tricarboxy ...
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Lysine
Lysine (symbol Lys or K) is an α-amino acid that is a precursor to many proteins. It contains an α-amino group (which is in the protonated form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain lysyl ((CH2)4NH2), classifying it as a basic, charged (at physiological pH), aliphatic amino acid. It is encoded by the codons AAA and AAG. Like almost all other amino acids, the α-carbon is chiral and lysine may refer to either enantiomer or a racemic mixture of both. For the purpose of this article, lysine will refer to the biologically active enantiomer L-lysine, where the α-carbon is in the ''S'' configuration. The human body cannot synthesize lysine. It is essential in humans and must therefore be obtained from the diet. In organisms that synthesise lysine, two main biosynthetic pathways exist, the diaminopimelate and α-aminoadipate pathways, which employ distinct e ...
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Krebs Cycle
The citric acid cycle (CAC)—also known as the Krebs cycle or the TCA cycle (tricarboxylic acid cycle)—is a series of chemical reactions to release stored energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins. The Krebs cycle is used by organisms that respire (as opposed to organisms that ferment) to generate energy, either by anaerobic respiration or aerobic respiration. In addition, the cycle provides precursors of certain amino acids, as well as the reducing agent NADH, that are used in numerous other reactions. Its central importance to many biochemical pathways suggests that it was one of the earliest components of metabolism and may have originated abiogenically. Even though it is branded as a 'cycle', it is not necessary for metabolites to follow only one specific route; at least three alternative segments of the citric acid cycle have been recognized. The name of this metabolic pathway is derived from the citric acid (a tricarbo ...
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Gibbs Free Energy
In thermodynamics, the Gibbs free energy (or Gibbs energy; symbol G) is a thermodynamic potential that can be used to calculate the maximum amount of work that may be performed by a thermodynamically closed system at constant temperature and pressure. It also provides a necessary condition for processes such as chemical reactions that may occur under these conditions. The Gibbs free energy change , measured in joules in SI) is the ''maximum'' amount of non-expansion work that can be extracted from a closed system (one that can exchange heat and work with its surroundings, but not matter) at fixed temperature and pressure. This maximum can be attained only in a completely reversible process. When a system transforms reversibly from an initial state to a final state under these conditions, the decrease in Gibbs free energy equals the work done by the system to its surroundings, minus the work of the pressure forces. The Gibbs energy is the thermodynamic potential that is minim ...
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Succinyl CoA
Succinyl-coenzyme A, abbreviated as succinyl-CoA () or SucCoA, is a thioester of succinic acid and coenzyme A. Sources It is an important intermediate in the citric acid cycle, where it is synthesized from α-ketoglutarate by α-ketoglutarate dehydrogenase through decarboxylation. During the process, coenzyme A is added. With B12 as an enzymatic cofactor, it is also synthesized from propionyl CoA, the odd-numbered fatty acid, which cannot undergo beta-oxidation. Propionyl-CoA is carboxylated to D-methylmalonyl-CoA, isomerized to L-methylmalonyl-CoA, and rearranged to yield succinyl-CoA via a vitamin B12-dependent enzyme. While Succinyl-CoA is an intermediate of the citric acid cycle, it cannot be readily incorporated there because there is no net consumption of Succinyl-CoA. Succinyl-CoA is first converted to malate, and then to pyruvate where it is then transported to the matrix to enter the citric acid cycle. Fate It is converted into succinate through the hydrolytic releas ...
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Redox
Redox (reduction–oxidation, , ) is a type of chemical reaction in which the oxidation states of substrate (chemistry), substrate change. Oxidation is the loss of Electron, electrons or an increase in the oxidation state, while reduction is the gain of electrons or a decrease in the oxidation state. There are two classes of redox reactions: * ''Electron-transfer'' – Only one (usually) electron flows from the reducing agent to the oxidant. This type of redox reaction is often discussed in terms of redox couples and electrode potentials. * ''Atom transfer'' – An atom transfers from one substrate to another. For example, in the rusting of iron, the oxidation state of iron atoms increases as the iron converts to an oxide, and simultaneously the oxidation state of oxygen decreases as it accepts electrons released by the iron. Although oxidation reactions are commonly associated with the formation of oxides, other chemical species can serve the same function. In hydrogen ...
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Decarboxylation
Decarboxylation is a chemical reaction that removes a carboxyl group and releases carbon dioxide (CO2). Usually, decarboxylation refers to a reaction of carboxylic acids, removing a carbon atom from a carbon chain. The reverse process, which is the first chemical step in photosynthesis, is called carboxylation, the addition of CO2 to a compound. Enzymes that catalyze decarboxylations are called decarboxylases or, the more formal term, carboxy-lyases (Enzyme Commission number, EC number 4.1.1). In organic chemistry The term "decarboxylation" usually means replacement of a carboxyl group () with a hydrogen atom: :RCO2H -> RH + CO2 Decarboxylation is one of the oldest known organic reactions. It is one of the processes assumed to accompany pyrolysis and destructive distillation. Metal salts, especially copper compounds, facilitate the reaction via the intermediacy of metal carboxylate complexes. Decarboxylation of aryl carboxylates can generate the equivalent of the correspond ...
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Oxoglutarate Dehydrogenase (α-Ketoglutarate Dehydrogenase)
The oxoglutarate dehydrogenase complex (OGDC) or α-ketoglutarate dehydrogenase complex is an enzyme complex, most commonly known for its role in the citric acid cycle. Units Much like pyruvate dehydrogenase complex (PDC), this enzyme forms a complex composed of three components: Three classes of these multienzyme complexes have been characterized: one specific for pyruvate, a second specific for 2-oxoglutarate, and a third specific for branched-chain α-keto acids. The oxoglutarate dehydrogenase complex has the same subunit structure and thus uses the same coenzymes as the pyruvate dehydrogenase complex and the branched-chain alpha-keto acid dehydrogenase complex (TTP, CoA, lipoate, FAD and NAD). Only the E3 subunit is shared in common between the three enzymes. Properties Metabolic pathways This enzyme participates in three different pathways: * Citric acid cycle (KEGG linkMAP00020 * Lysine degradation (KEGG linkMAP00310 * Tryptophan metabolism (KEGG linkMAP00380 Kine ...
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NADH
Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD and NADH (H for hydrogen), respectively. In metabolism, nicotinamide adenine dinucleotide is involved in redox reactions, carrying electrons from one reaction to another. The cofactor is, therefore, found in two forms in cells: NAD is an oxidizing agent – it accepts electrons from other molecules and becomes reduced. This reaction, also with H+, forms NADH, which can then be used as a reducing agent to donate electrons. These electron transfer reactions are the main function of NAD. However, it is also used in other cellular processes, most notably as a substrate of enzymes in adding or removing chemical groups t ...
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Carbon Dioxide
Carbon dioxide (chemical formula ) is a chemical compound made up of molecules that each have one carbon atom covalently double bonded to two oxygen atoms. It is found in the gas state at room temperature. In the air, carbon dioxide is transparent to visible light but absorbs infrared radiation, acting as a greenhouse gas. It is a trace gas in Earth's atmosphere at 421 parts per million (ppm), or about 0.04% by volume (as of May 2022), having risen from pre-industrial levels of 280 ppm. Burning fossil fuels is the primary cause of these increased CO2 concentrations and also the primary cause of climate change.IPCC (2022Summary for policy makersiClimate Change 2022: Mitigation of Climate Change. Contribution of Working Group III to the Sixth Assessment Report of the Intergovernmental Panel on Climate Change Cambridge University Press, Cambridge, United Kingdom and New York, NY, USA Carbon dioxide is soluble in water and is found in groundwater, lakes, ice caps, ...
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Succinyl CoA
Succinyl-coenzyme A, abbreviated as succinyl-CoA () or SucCoA, is a thioester of succinic acid and coenzyme A. Sources It is an important intermediate in the citric acid cycle, where it is synthesized from α-ketoglutarate by α-ketoglutarate dehydrogenase through decarboxylation. During the process, coenzyme A is added. With B12 as an enzymatic cofactor, it is also synthesized from propionyl CoA, the odd-numbered fatty acid, which cannot undergo beta-oxidation. Propionyl-CoA is carboxylated to D-methylmalonyl-CoA, isomerized to L-methylmalonyl-CoA, and rearranged to yield succinyl-CoA via a vitamin B12-dependent enzyme. While Succinyl-CoA is an intermediate of the citric acid cycle, it cannot be readily incorporated there because there is no net consumption of Succinyl-CoA. Succinyl-CoA is first converted to malate, and then to pyruvate where it is then transported to the matrix to enter the citric acid cycle. Fate It is converted into succinate through the hydrolytic releas ...
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