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Maltase
Maltase is an informal name for a family of enzymes that catalyze the hydrolysis of disaccharide maltose into two simple sugars of glucose. Maltases are found in plants, bacteria, yeast, humans, and other vertebrates. Digestion of starch requires six intestinal enzymes. Two of these enzymes are luminal endo-glucosidases named alpha-amylases. The other four enzymes have been identified as different maltases, exo-glucosidases bound to the luminal surface of enterocytes. Two of these maltase activities were associated with sucrase-isomaltase (maltase Ib, maltase Ia). The other two maltases with no distinguishing characteristics were named maltase-glucoamylase (maltases II and III). The activities of these four maltases are also described as alpha-glucosidase because they all digest linear starch oligosaccharides to glucose. Structure Maltases are members of a group of intestinal enzymes called FamilyGH13 (Glycoside hydrolase family 13) that are responsible for breaking apart the ...
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Sucrase-isomaltase
Sucrase-isomaltase is a bifunctional glucosidase (sugar-digesting enzyme) located on the brush border of the small intestine, encoded by the human gene ''SI''. It is a dual-function enzyme with two GH31 domains, one serving as the isomaltase, the other as a sucrose alpha-glucosidase. It has preferential expression in the apical membranes of enterocytes. The enzyme’s purpose is to digest dietary carbohydrates such as starch, sucrose and isomaltose. By further processing the broken-down products, energy in the form of ATP can be generated. Structure Sucrase-isomaltase consists of two enzymatic subunits: sucrase and isomaltase. The subunits originate from a polypeptide precursor, pro-SI. By heterodimerizing the two subunits, the sucrase-isomaltase complex is formed. The enzyme is anchored in the intestinal brush border membrane by a hydrophobic segment located near the N-terminus of the isomaltase subunit. Before the enzyme is anchored to the membrane, pro-SI is mannose-rich an ...
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Maltase Reaction
Maltase is an informal name for a family of enzymes that catalyze the hydrolysis of disaccharide maltose into two simple sugars of glucose. Maltases are found in plants, bacteria, yeast, humans, and other vertebrates. Digestion of starch requires six intestinal enzymes. Two of these enzymes are luminal endo-glucosidases named alpha-amylases. The other four enzymes have been identified as different maltases, exo-glucosidases bound to the luminal surface of enterocytes. Two of these maltase activities were associated with sucrase-isomaltase (maltase Ib, maltase Ia). The other two maltases with no distinguishing characteristics were named maltase-glucoamylase (maltases II and III). The activities of these four maltases are also described as alpha-glucosidase because they all digest linear starch oligosaccharides to glucose. Structure Maltases are members of a group of intestinal enzymes called FamilyGH13 (Glycoside hydrolase family 13) that are responsible for breaking apart th ...
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Maltose Structure
} Maltose ( or ), also known as maltobiose or malt sugar, is a disaccharide formed from two units of glucose joined with an α(1→4) bond. In the isomer isomaltose, the two glucose molecules are joined with an α(1→6) bond. Maltose is the two-unit member of the amylose homologous series, the key structural motif of starch. When beta-amylase breaks down starch, it removes two glucose units at a time, producing maltose. An example of this reaction is found in germinating seeds, which is why it was named after malt. Unlike sucrose, it is a reducing sugar. History Maltose was discovered by Augustin-Pierre Dubrunfaut, although this discovery was not widely accepted until it was confirmed in 1872 by Irish chemist and brewer Cornelius O'Sullivan. Its name comes from malt, combined with the suffix ' -ose' which is used in names of sugars. Structure and nomenclature Carbohydrates are generally divided into monosaccharides, oligosaccharides, and polysaccharides depending on th ...
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Acid Maltase Deficiency
Glycogen storage disease type II (GSD-II), also called Pompe disease, and formerly known as GSD-IIa or Limb–girdle muscular dystrophy 2V, is an autosomal recessive metabolic disorder which damages muscle and nerve cells throughout the body. It is caused by an accumulation of glycogen in the lysosome due to a deficiency of the lysosomal acid alpha-glucosidase enzyme (GAA). The inability to break down glycogen within the lysosomes of cells leads to progressive muscle weakness throughout the body and affects various body tissues, particularly in the heart, skeletal muscles, liver and the nervous system. GSD-II and Danon disease are the only glycogen storage diseases characterised by a defect in lysosomal metabolism. It was first identified in 1932 by Dutch pathologist Joannes Cassianus Pompe, making it the first glycogen storage disease to be discovered. Signs and symptoms Infantile-Onset (IOPD) The infantile-onset (IOPD) form usually comes to medical attention within the fi ...
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Glucose
Glucose is a sugar with the Chemical formula#Molecular formula, molecular formula , which is often abbreviated as Glc. It is overall the most abundant monosaccharide, a subcategory of carbohydrates. It is mainly made by plants and most algae during photosynthesis from water and carbon dioxide, using energy from sunlight. It is used by plants to make cellulose, the most abundant carbohydrate in the world, for use in cell walls, and by all living Organism, organisms to make adenosine triphosphate (ATP), which is used by the cell as energy. In energy metabolism, glucose is the most important source of energy in all organisms. Glucose for metabolism is stored as a polymer, in plants mainly as amylose and amylopectin, and in animals as glycogen. Glucose circulates in the blood of animals as blood sugar. The naturally occurring form is -glucose, while its Stereoisomerism, stereoisomer L-glucose, -glucose is produced synthetically in comparatively small amounts and is less biologicall ...
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Acid Alpha-glucosidase
Acid alpha-glucosidase, also called acid maltase, is an enzyme that helps to break down glycogen in the lysosome. It is functionally similar to glycogen debranching enzyme, but is on a different chromosome, processed differently by the cell and is located in the lysosome rather than the cytosol. In humans, it is encoded by the ''GAA'' gene. Errors in this gene cause glycogen storage disease type II (Pompe disease). Function This gene encodes lysosomal alpha-glucosidase, which is essential for the degradation of glycogen to glucose in lysosome A lysosome () is a membrane-bound organelle that is found in all mammalian cells, with the exception of red blood cells (erythrocytes). There are normally hundreds of lysosomes in the cytosol, where they function as the cell’s degradation cent ...s. Different forms of acid alpha-glucosidase are obtained by proteolytic processing. Defects in this gene are the cause of glycogen storage disease II, also known as Pompe disease, which is ...
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Alzheimer's Disease
Alzheimer's disease (AD) is a neurodegenerative disease and the cause of 60–70% of cases of dementia. The most common early symptom is difficulty in remembering recent events. As the disease advances, symptoms can include problems with language, disorientation (including easily getting lost), mood swings, loss of motivation, self-neglect, and behavioral issues. As a person's condition declines, they often withdraw from family and society. Gradually, bodily functions are lost, ultimately leading to death. Although the speed of progression can vary, the average life expectancy following diagnosis is three to twelve years. The causes of Alzheimer's disease remain poorly understood. There are many environmental and genetic risk factors associated with its development. The strongest genetic risk factor is from an allele of apolipoprotein E. Other risk factors include a history of head injury, clinical depression, and high blood pressure. The progression of the di ...
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AMY1A
Alpha-amylase 1 is an enzyme that in humans is encoded by the polich gene In biology, the word gene has two meanings. The Mendelian gene is a basic unit of heredity. The molecular gene is a sequence of nucleotides in DNA that is transcribed to produce a functional RNA. There are two types of molecular genes: protei .... This gene is found in many organisms. Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and glycogen. The human genome has a cluster of several amylase genes that are expressed at high levels in either salivary gland or pancreas. This gene encodes an amylase isoenzyme produced by the salivary gland. Alternative splicing results in multiple transcript variants encoding the same protein. See also * AMY2A * References External links * * Further reading

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Cellular Respiration
Cellular respiration is the process of oxidizing biological fuels using an inorganic electron acceptor, such as oxygen, to drive production of adenosine triphosphate (ATP), which stores chemical energy in a biologically accessible form. Cellular respiration may be described as a set of metabolic reactions and processes that take place in the cells of organisms to transfer chemical energy from nutrients to ATP, with the flow of electrons to an electron acceptor, and then release waste products. If the electron acceptor is oxygen, the process is more specifically known as aerobic cellular respiration. If the electron acceptor is a molecule other than oxygen, this is anaerobic cellular respiration. Fermentation, which is also an anaerobic process, is not respiration, as no external electron acceptor is involved. The reactions involved in respiration are catabolic reactions, which break large molecules into smaller ones, producing large amounts of energy (ATP). Respiration ...
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