Dihydrolipoamide
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Dihydrolipoamide
Dihydrolipoamide is a molecule oxidized by dihydrolipoyl dehydrogenase in order to produce lipoamide. Lipoamide is subsequently used as a cofactor for α-ketoglutarate dehydrogenase, the pyruvate dehydrogenase complex, and branched-chain α-ketoacid dehydrogenase complex. See also * Dihydrolipoic acid * Lipoic acid Lipoic acid (LA), also known as α-lipoic acid, alpha-lipoic acid (ALA) and thioctic acid, is an organosulfur compound derived from caprylic acid (octanoic acid). ALA is made in animals normally, and is essential for aerobic metabolism. It is a ... References Carboxamides Thiols {{organic-compound-stub ...
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Dihydrolipoyl Dehydrogenase
Dihydrolipoamide dehydrogenase (DLD), also known as dihydrolipoyl dehydrogenase, mitochondrial, is an enzyme that in humans is encoded by the ''DLD'' gene. DLD is a flavoprotein enzyme that oxidizes dihydrolipoamide to lipoamide. Dihydrolipoamide dehydrogenase (DLD) is a mitochondrial enzyme that plays a vital role in energy metabolism in eukaryotes. This enzyme is required for the complete reaction of at least five different multi-enzyme complexes. Additionally, DLD is a flavoenzyme oxidoreductase that contains a reactive disulfide bridge and a FAD cofactor that are directly involved in catalysis. The enzyme associates into tightly bound homodimers required for its enzymatic activity. File:Lipoamide-2D-skeletal.png, Lipoamide File:Dihydrolipoamide.svg, Dihydrolipoamide Structure The protein encoded by the DLD gene comes together with another protein to form a dimer in the central metabolic pathway. Several amino acids within the catalytic pocket have been identified as ...
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Pyruvate Dehydrogenase Complex
Pyruvate dehydrogenase complex (PDC) is a complex of three enzymes that converts pyruvate into acetyl-CoA by a process called pyruvate decarboxylation. Acetyl-CoA may then be used in the citric acid cycle to carry out cellular respiration, and this complex links the glycolysis metabolic pathway to the citric acid cycle. Pyruvate decarboxylation is also known as the "pyruvate dehydrogenase reaction" because it also involves the oxidation of pyruvate. This multi-enzyme complex is related structurally and functionally to the oxoglutarate dehydrogenase and branched-chain oxo-acid dehydrogenase multi-enzyme complexes. Reaction The reaction catalysed by pyruvate dehydrogenase complex is: Structure Pyruvate dehydrogenase (E1) The E1 subunit, called the pyruvate dehydrogenase subunit, has a structure that consists of two chains (an “ɑ” and “ꞵ” chain). A magnesium ion forms a 4-coordinate complex with three, polar amino acid residues (Asp, Asn, and Tyr) located on t ...
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Branched-chain α-ketoacid Dehydrogenase Complex
The branched-chain α-ketoacid dehydrogenase complex (BCKDC or BCKDH complex) is a multi-subunit complex of enzymes that is found on the mitochondrial inner membrane. This enzyme complex catalyzes the oxidative decarboxylation of branched, short-chain alpha-ketoacids. BCKDC is a member of the mitochondrial α-ketoacid dehydrogenase complex family comprising pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase, key enzymes that function in the Krebs cycle. Coenzymes This complex requires the following 5 coenzymes: * Thiamine pyrophosphate * Lipoate (lipoic acid) * Coenzyme A * Flavin adenine dinucleotide (FAD) * Nicotinamide adenine dinucleotide (NAD+) Biological function In animal tissue, BCKDC catalyzes an irreversible step in the catabolism of the branched-chain amino acids L-isoleucine, L-valine, and L-leucine, acting on their deaminated derivatives (L-alpha-keto-beta-methylvalerate, alpha-ketoisovalerate, and alpha-ketoisocaproate, respectively) and converting ...
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Lipoic Acid
Lipoic acid (LA), also known as α-lipoic acid, alpha-lipoic acid (ALA) and thioctic acid, is an organosulfur compound derived from caprylic acid (octanoic acid). ALA is made in animals normally, and is essential for aerobic metabolism. It is also manufactured and is available as a dietary supplement in some countries where it is marketed as an antioxidant, and is available as a pharmaceutical drug in other countries. Lipoate is the conjugate base of lipoic acid, and the most prevalent form of LA under physiological conditions. Only the (''R'')-(+)-enantiomer (RLA) exists in nature and is essential for aerobic metabolism because RLA is an essential cofactor of many enzyme complexes. Physical and chemical properties Lipoic acid (LA), also known as α-lipoic acid, alpha-lipoic acid (ALA), and thioctic acid is an organosulfur compound derived from octanoic acid. LA contains two sulfur atoms (at C6 and C8) connected by a disulfide bond and is thus considered to be oxidized althou ...
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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 Kinet ...
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Royal Society Of Chemistry
The Royal Society of Chemistry (RSC) is a learned society (professional association) in the United Kingdom with the goal of "advancing the chemistry, chemical sciences". It was formed in 1980 from the amalgamation of the Chemical Society, the Royal Institute of Chemistry, the Faraday Society, and the Society for Analytical Chemistry with a new Royal Charter and the dual role of learned society and professional body. At its inception, the Society had a combined membership of 34,000 in the UK and a further 8,000 abroad. The headquarters of the Society are at Burlington House, Piccadilly, London. It also has offices in Thomas Graham House in Cambridge (named after Thomas Graham (chemist), Thomas Graham, the first president of the Chemical Society) where ''RSC Publishing'' is based. The Society has offices in the United States, on the campuses of The University of Pennsylvania and Drexel University, at the University City Science Center in Philadelphia, Pennsylvania, in both Beijing a ...
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Lipoamide
Lipoamide is a trivial name for 6,8-dithiooctanoic amide. It is the functional form of lipoic acid, i.e the carboxyl group is attached to protein via an amine with an amide linkage. Illustrative of the biochemical role of lipoamide is in the conversion of pyruvate to acetyl lipoamide. Lipoamide is found in a large number of plant and animal-based foods. See also * Lipoic acid Lipoic acid (LA), also known as α-lipoic acid, alpha-lipoic acid (ALA) and thioctic acid, is an organosulfur compound derived from caprylic acid (octanoic acid). ALA is made in animals normally, and is essential for aerobic metabolism. It is a ... References External links * Organic disulfides Carboxamides {{Organic-compound-stub ...
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Dihydrolipoic Acid
Dihydrolipoic acid is an organic compound that is the reduced form of lipoic acid. This carboxylic acid features a pair of thiol groups, and therefore is a dithiol. It is optically active, but only the R-enantiomer is biochemically significant. The lipoic acid/dihydrolipoic acid pair participate in a variety of biochemical transformations. See also * Dihydrolipoamide * Lipoamide Lipoamide is a trivial name for 6,8-dithiooctanoic amide. It is the functional form of lipoic acid, i.e the carboxyl group is attached to protein via an amine with an amide linkage. Illustrative of the biochemical role of lipoamide is in the conve ... References {{Reflist Carboxylic acids Thiols ...
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