Pentose Phosphate Pathway
The pentose phosphate pathway (also called the phosphogluconate pathway and the hexose monophosphate shunt or HMP shunt) is a metabolic pathway parallel to glycolysis. It generates NADPH and pentoses (five-carbon sugars) as well as ribose 5-phosphate, a precursor for the synthesis of nucleotides. While the pentose phosphate pathway does involve oxidation of glucose, its primary role is anabolic rather than catabolic. The pathway is especially important in red blood cells (erythrocytes). The reactions of the pathway were elucidated in the early 1950s by Bernard Horecker and co-workers. There are two distinct phases in the pathway. The first is the oxidative phase, in which NADPH is generated, and the second is the non-oxidative synthesis of five-carbon sugars. For most organisms, the pentose phosphate pathway takes place in the cytosol; in plants, most steps take place in plastids. Like glycolysis, the pentose phosphate pathway appears to have a very ancient evolutionary ori ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Pentose Phosphate Pathway En
In chemistry, a pentose is a monosaccharide (simple sugar) with five carbon atoms. The chemical formula of many pentoses is , and their molecular weight is 150.13 g/mol.-Ribose . PubChem compound webpage, accessed on 2010-02-06. Pentoses are very important in . is a constituent of , and the related molecule, , is a constituent of [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Plastid
A plastid is a membrane-bound organelle found in the Cell (biology), cells of plants, algae, and some other eukaryotic organisms. Plastids are considered to be intracellular endosymbiotic cyanobacteria. Examples of plastids include chloroplasts (used for photosynthesis); chromoplasts (used for synthesis and storage of pigments); leucoplasts (non-pigmented plastids, some of which can cellular differentiation, differentiate); and apicoplasts (non-photosynthetic plastids of apicomplexa derived from secondary endosymbiosis). A permanent primary endosymbiosis event occurred about 1.5 billion years ago in the Archaeplastida cladeEmbryophyte, land plants, red algae, green algae and glaucophytesprobably with a cyanobiont, a symbiotic cyanobacteria related to the genus ''Gloeomargarita lithophora, Gloeomargarita''. Another primary endosymbiosis event occurred later, between 140 and 90 million years ago, in the photosynthetic plastids ''Paulinella'' amoeboids of the cyanobacteria genera '' ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Glutathione Peroxidase
Glutathione peroxidase (GPx) () is the general name of an enzyme family with peroxidase activity whose main biological role is to protect the organism from oxidative damage. The biochemical function of glutathione peroxidase is to reduce lipid hydroperoxides to their corresponding alcohols and to reduce free hydrogen peroxide to water. Glutathione peroxidase was discovered in 1957 by Gordon C. Mills. Reaction The main reaction that glutathione peroxidase catalyzes is: : 2GSH + H2O2 → GS–SG + 2H2O where GSH represents reduced monomeric glutathione, and GS–SG represents glutathione disulfide. The mechanism involves oxidation of the selenol of a selenocysteine residue by hydrogen peroxide. This process gives the derivative with a selenenic acid (RSeOH) group. The selenenic acid is then converted back to the selenol by a two step process that begins with reaction with GSH to form the GS-SeR and water. A second GSH molecule reduces the GS-SeR intermediate back to t ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Glutathione Reductase
Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that in humans is encoded by the GSR gene. Glutathione reductase (EC 1.8.1.7) catalyzes the reduction of glutathione disulfide ( GSSG) to the sulfhydryl form glutathione ( GSH), which is a critical molecule in resisting oxidative stress and maintaining the reducing environment of the cell. Glutathione reductase functions as dimeric disulfide oxidoreductase and utilizes an FAD prosthetic group and NADPH to reduce one molar equivalent of GSSG to two molar equivalents of GSH: The glutathione reductase is conserved between all kingdoms. In bacteria, yeasts, and animals, one glutathione reductase gene is found; however, in plant genomes, two GR genes are encoded. ''Drosophila'' and trypanosomes do not have any GR at all. In these organisms, glutathione reduction is performed by either the thioredoxin or the trypanothione system, respectively. Function Glutathione plays a key role in m ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Glutathione
Glutathione (GSH, ) is an organic compound with the chemical formula . It is an antioxidant in plants, animals, fungi, and some bacteria and archaea. Glutathione is capable of preventing damage to important cellular components caused by sources such as reactive oxygen species, free radicals, peroxides, lipid peroxides, and heavy metals. It is a tripeptide with a gamma peptide linkage between the carboxyl group of the glutamate side chain and cysteine. The carboxyl group of the cysteine residue is attached by normal peptide linkage to glycine. Biosynthesis and occurrence Glutathione biosynthesis involves two adenosine triphosphate-dependent steps: *First, γ-glutamylcysteine is synthesized from L-glutamate and L-cysteine. This conversion requires the enzyme glutamate–cysteine ligase (GCL, glutamate cysteine synthase). This reaction is the rate-limiting step in glutathione synthesis. *Second, glycine is added to the C-terminal of γ-glutamylcysteine. This condensation is ca ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Oxidative Stress
Oxidative stress reflects an imbalance between the systemic manifestation of reactive oxygen species and a biological system's ability to readily detoxify the reactive intermediates or to repair the resulting damage. Disturbances in the normal redox state of cells can cause toxic effects through the production of peroxides and free radicals that damage all components of the cell, including proteins, lipids, and DNA. Oxidative stress from oxidative metabolism causes base damage, as well as strand breaks in DNA. Base damage is mostly indirect and caused by the reactive oxygen species generated, e.g., (superoxide radical), OH ( hydroxyl radical) and (hydrogen peroxide). Further, some reactive oxidative species act as cellular messengers in redox signaling. Thus, oxidative stress can cause disruptions in normal mechanisms of cellular signaling. In humans, oxidative stress is thought to be involved in the development of attention deficit hyperactivity disorder, cancer, Parkin ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Reduction (chemistry)
Redox ( , , reduction–oxidation or oxidation–reduction) is a type of chemical reaction in which the oxidation states of the reactants change. Oxidation is the loss of electrons or an increase in the oxidation state, while reduction is the gain of electrons or a decrease in the oxidation state. The oxidation and reduction processes occur simultaneously in the chemical reaction. There are two classes of redox reactions: * Electron transfer, Electron-transfer – Only one (usually) electron flows from the atom, ion, or molecule being oxidized to the atom, ion, or molecule that is reduced. This type of redox reaction is often discussed in terms of redox couples and electrode potentials. * Atom transfer – An atom transfers from one Substrate (chemistry), 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 r ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Lignin
Lignin is a class of complex organic polymers that form key structural materials in the support tissues of most plants. Lignins are particularly important in the formation of cell walls, especially in wood and bark, because they lend rigidity and do not rot easily. Chemically, lignins are polymers made by cross-linking phenolic precursors. History Lignin was first mentioned in 1813 by the Swiss botanist A. P. de Candolle, who described it as a fibrous, tasteless material, insoluble in water and alcohol but soluble in weak alkaline solutions, and which can be precipitated from solution using acid. He named the substance "lignine", which is derived from the Latin word '' lignum'', meaning wood. It is one of the most abundant organic polymers on Earth, exceeded only by cellulose and chitin. Lignin constitutes 30% of terrestrial non-fossil organic carbon on Earth, and 20 to 35% of the dry mass of wood. Lignin is present in red algae, which suggest that the common ancestor ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Aromatic Amino Acid
An aromatic amino acid is an amino acid that includes an aromaticity, aromatic ring. Among the 20 standard amino acids, histidine, phenylalanine, tryptophan, tyrosine, are classified as aromatic. Properties and function Optical properties Aromatic amino acids, excepting histidine, absorb Ultraviolet, ultraviolet light above and beyond 250 nm and will fluorescence, fluoresce under these conditions. This characteristic is used in quantitative analysis, notably in determining the concentrations of these amino acids in solution. Most proteins Absorption spectroscopy, absorb at 280 nm due to the presence of tyrosine and tryptophan. Of the aromatic amino acids, tryptophan has the highest extinction coefficient; its absorption maximum occurs at 280 nm. The absorption maximum of tyrosine occurs at 274 nm. Role in protein structure and function Aromatic amino acids stabilize folded structures of many proteins. Aromatic residues are found predominantly sequestered within the cores o ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Erythrose 4-phosphate
Erythrose 4-phosphate is a phosphate of the simple sugar erythrose. It is an intermediate in the pentose phosphate pathway and the Calvin cycle. The enzyme transaldolase catalyzes the formation of erythrose 4-phosphate and fructose 6-phosphate from sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate. This reaction is a part of the non-oxidative phase of the pentose phosphate pathway. In the Calvin cycle, the enzyme fructose-bisphosphate aldolase catalyzes the formation of sedoheptulose 1,7-bisphosphate from erythrose 4-phosphate and dihydroxyacetone phosphate. In addition, it serves as a precursor in the biosynthesis of the aromatic amino acids tyrosine, phenylalanine, and tryptophan. It is used in the first step of the shikimate pathway. At this stage, phosphoenolpyruvate and erythrose-4-phosphate react to form 3-deoxy-D-arabinoheptulosonate-7-phosphate (DAHP), in a reaction catalyzed by the enzyme DAHP synthase. : It also used in 3-hydroxy-1-aminoacetone phosphat ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Nucleotide
Nucleotides are Organic compound, organic molecules composed of a nitrogenous base, a pentose sugar and a phosphate. They serve as monomeric units of the nucleic acid polymers – deoxyribonucleic acid (DNA) and ribonucleic acid (RNA), both of which are essential biomolecules within all Life, life-forms on Earth. Nucleotides are obtained in the diet and are also synthesized from common Nutrient, nutrients by the liver. Nucleotides are composed of three subunit molecules: a nucleobase, a pentose, five-carbon sugar (ribose or deoxyribose), and a phosphate group consisting of one to three phosphates. The four nucleobases in DNA are guanine, adenine, cytosine, and thymine; in RNA, uracil is used in place of thymine. Nucleotides also play a central role in metabolism at a fundamental, cellular level. They provide chemical energy—in the form of the nucleoside triphosphates, adenosine triphosphate (ATP), guanosine triphosphate (GTP), cytidine triphosphate (CTP), and uridine triph ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Fatty Acid Synthesis
In biochemistry, fatty acid synthesis is the creation of fatty acids from acetyl-CoA and NADPH through the action of enzymes. Two ''De novo synthesis, de novo'' fatty acid syntheses can be distinguished: cytosolic fatty acid synthesis (FAS/FASI) and mitochondrial fatty acid synthesis (mtFAS/mtFASII). Most of the acetyl-CoA which is converted into fatty acids is derived from carbohydrates via the Glycolysis, glycolytic pathway. The glycolytic pathway also provides the glycerol with which three fatty acids can combine (by means of Ester, ester bonds) to form Fat, triglycerides (also known as "triacylglycerols" – to distinguish them from fatty "acids" – or simply as "fat"), the final product of the Lipogenesis, lipogenic process. When only two fatty acids combine with glycerol and the third alcohol group is phosphorylated with a group such as phosphatidylcholine, a phospholipid is formed. Phospholipids form the bulk of the lipid bilayers that make up cell membranes and surrounds t ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |