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List Of MeSH Codes (D05)
The following is a partial list of the "D" codes for Medical Subject Headings (MeSH), as defined by the United States National Library of Medicine (NLM). This list continues the information at List of MeSH codes (D04). Codes following these are found at List of MeSH codes (D06). For other MeSH codes, see List of MeSH codes. The source for this content is the set o2006 MeSH Treesfrom the NLM. – macromolecular substances – dendrimers – multiprotein complexes – amyloid – dystrophin-associated protein complex – light-harvesting protein complexes * – phycobilisomes – molecular motors – multienzyme complexes * – cytochrome b6f complex * – plastoquinol-plastocyanin reductase * – electron transport complex i * – electron transport complex iv * – fatty acid synthetase complex * – glycine decarboxylase complex * – aminomethyltransferase * – dihydrolipoamide dehydrogenase * – glycine decarboxylase complex h-protein * – glycine ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Medical Subject Headings
Medical Subject Headings (MeSH) is a comprehensive controlled vocabulary for the purpose of indexing Academic journal, journal articles and books in the Life science, life sciences. It serves as a thesaurus of index terms that facilitates searching. Created and updated by the United States National Library of Medicine (NLM), it is used by the MEDLINE/PubMed article database and by NLM's catalog of book holdings. MeSH is also used by ClinicalTrials.gov registry to classify which diseases are studied by trials registered in ClinicalTrials. MeSH was introduced in the 1960s, with the NLM's own index catalogue and the subject headings of the Quarterly Cumulative Index Medicus (1940 edition) as precursors. The yearly printed version of MeSH was discontinued in 2007; MeSH is now available only online. It can be browsed and downloaded free of charge through PubMed. Originally in English, MeSH has been translated into numerous other languages and allows retrieval of documents from differ ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Electron Transport Complex Iv
An electron transport chain (ETC) is a series of protein complexes and other molecules which transfer electrons from electron donors to electron acceptors via redox reactions (both reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H+ ions) across a membrane. Many of the enzymes in the electron transport chain are embedded within the membrane. The flow of electrons through the electron transport chain is an exergonic process. The energy from the redox reactions creates an electrochemical proton gradient that drives the synthesis of adenosine triphosphate (ATP). In aerobic respiration, the flow of electrons terminates with molecular oxygen as the final electron acceptor. In anaerobic respiration, other electron acceptors are used, such as sulfate. In an electron transport chain, the redox reactions are driven by the difference in the Gibbs free energy of reactants and products. The free energy released when a higher-e ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Dihydrolipoyllysine-residue Acetyltransferase
Dihydrolipoyl transacetylase (or dihydrolipoamide acetyltransferase) is an enzyme component of the multienzyme pyruvate dehydrogenase complex. The pyruvate dehydrogenase complex is responsible for the pyruvate decarboxylation step that links glycolysis to the citric acid cycle. This involves the transformation of pyruvate from glycolysis into acetyl-CoA Acetyl-CoA (acetyl coenzyme A) is a molecule that participates in many biochemical reactions in protein, carbohydrate and lipid metabolism. Its main function is to deliver the acetyl group to the citric acid cycle (Krebs cycle) to be oxidation, o ... which is then used in the citric acid cycle to carry out cellular respiration. There are three different enzyme components in the pyruvate dehydrogenase complex. Pyruvate dehydrogenase (EC 1.2.4.1) is responsible for the oxidation of pyruvate, dihydrolipoyl transacetylase (this enzyme; EC 2.3.1.12) transfers the acetyl group to coenzyme A (CoA), and dihydrolipoyl dehydrogenase (EC ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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. The levels of pyruvate dehydrogenase enzymes play a major role in regulating the rate of carbohydrate metabolism and are strongly stimulated by the evolutionarily ancient hormone insulin. The PDC is opposed by the activity of pyruvate dehydrogenase kinase, and this mechanism plays a pivotal role in regulating rates of carbohydrate and lipid metabolism in many physiological states across taxa, including feeding, starvation, diabetes mellitus, hyperthyroidism, and hibernation. The multi-enzyme complex is related structurally and fun ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proteasome Endopeptidase Complex
Proteasome endopeptidase complex (, ''ingensin'', ''macropain'', ''multicatalytic endopeptidase complex'', ''prosome'', ''multicatalytic proteinase (complex)'', ''MCP'', ''proteasome'', ''large multicatalytic protease'', ''proteasome organelle'', ''alkaline protease'', ''26S protease'', ''tricorn proteinase'', ''tricorn protease'') is an enzyme. This enzyme catalyses the following chemical reaction : Cleavage of peptide bond In organic chemistry, a peptide bond is an amide type of covalent chemical bond linking two consecutive alpha-amino acids from C1 (carbon number one) of one alpha-amino acid and N2 (nitrogen number two) of another, along a peptide or protein cha ...s with very broad specificity This 20-S protein is composed of 28 subunits arranged in four rings of seven. References External links * {{Portal bar, Biology, border=no EC 3.4.25 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Photosystem Ii Protein Complex
Photosystems are functional and structural units of protein complexes involved in photosynthesis. Together they carry out the primary photochemistry of photosynthesis: the absorption of light and the transfer of energy and electrons. Photosystems are found in the thylakoid membranes of plants, algae, and cyanobacteria. These membranes are located inside the chloroplasts of plants and algae, and in the cytoplasmic membrane of photosynthetic bacteria. There are two kinds of photosystems: PSI and PSII. PSII will absorb red light, and PSI will absorb far-red light. Although photosynthetic activity will be detected when the photosystems are exposed to either red or far-red light, the photosynthetic activity will be the greatest when plants are exposed to both wavelengths of light. Studies have actually demonstrated that the two wavelengths together have a synergistic effect on the photosynthetic activity, rather than an additive one.Each photosystem has two parts: a reaction center, whe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phosphoenolpyruvate Sugar Phosphotransferase System
Phosphoenolpyruvate (2-phosphoenolpyruvate, PEP) is the carboxylic acid derived from the enol of pyruvate and a phosphate anion. It exists as an anion. PEP is an important intermediate in biochemistry. It has the highest-energy phosphate bond found (−61.9 kJ/mol) in organisms, and is involved in glycolysis and gluconeogenesis. In plants, it is also involved in the biosynthesis of various aromatic compounds, and in carbon fixation; in bacteria, it is also used as the source of energy for the phosphotransferase system. In glycolysis PEP is formed by the action of the enzyme enolase on 2-phosphoglyceric acid. Metabolism of PEP to pyruvic acid by pyruvate kinase (PK) generates adenosine triphosphate (ATP) via substrate-level phosphorylation. ATP is one of the major currencies of chemical energy within cells. In gluconeogenesis PEP is formed from the decarboxylation of oxaloacetate and hydrolysis of one guanosine triphosphate molecule. This reaction is catalyzed by the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ketoglutarate Dehydrogenase Complex
Ketoglutaric acid or oxoglutaric acid, or its conjugate base, the carboxylate ketoglutarate or oxoglutarate, may refer to the following chemical compounds: * α-Ketoglutaric acid, an intermediate in the citric acid cycle The citric acid cycle—also known as the Krebs cycle, Szent–Györgyi–Krebs cycle, or TCA cycle (tricarboxylic acid cycle)—is a series of chemical reaction, biochemical reactions that release the energy stored in nutrients through acetyl-Co ... * β-Ketoglutaric acid (acetonedicarboxylic acid or 3-oxoglutaric acid) {{Chemistry index ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycine Dehydrogenase (decarboxylating)
Glycine decarboxylase also known as glycine cleavage system P protein or glycine dehydrogenase is an enzyme that in humans is encoded by the ''GLDC'' gene. Reaction Glycine decarboxylase () is an enzyme that catalyzes the following chemical reaction: :glycine + H-protein-lipoyllysine \rightleftharpoons H-protein-S-aminomethyldihydrolipoyllysine + CO2 Thus, the two substrates of this enzyme are glycine and H-protein-lipoyllysine, whereas its two products are H-protein-S-aminomethyldihydrolipoyllysine and CO2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with a disulfide as acceptor. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate. Function Glycine decarboxylase is the P-protein of the glycine cleavage system in eukaryotes. The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of gl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycine Decarboxylase Complex H-protein
Glycine (symbol Gly or G; ) is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). Glycine disrupts the formation of alpha-helices in secondary protein structure. Its small side chain causes it to favor random coils instead. Glycine is also an inhibitory neurotransmitter – interference with its release within the spinal cord (such as during a ''Clostridium tetani'' infection) can cause spastic paralysis due to uninhibited muscle contraction. It is the only achiral proteinogenic amino acid. It can fit into both hydrophilic and hydrophobic environments, due to its minimal side chain of only one hydrogen atom. History and etymology Glycine was discovered in 1820 by French chemist Henri Braconnot when he hydrolyzed gelatin by boiling it with sulfuric acid. He originally called it "sugar of gelatin", but Fr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Dihydrolipoamide 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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
