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Neuraminidase
Exo-α-sialidase (, sialidase, neuraminidase; systematic name acetylneuraminyl hydrolase) is a glycoside hydrolase that cleaves the glycosidic linkages of neuraminic acids: : Hydrolysis of α-(2→3)-, α-(2→6)-, α-(2→8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates Neuraminidase Enzyme, enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. Viral neuraminidase was the first neuraminidase to be identified. It was discovered in 1957 by Alfred Gottschalk (biochemist), Alfred Gottschalk at the WEHI, Walter and Eliza Hall Institute in Melbourne. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Ot ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Viral Neuraminidase
Viral neuraminidase is a type of neuraminidase found on the surface of influenza viruses that enables the virus to be released from the host cell. Neuraminidases are enzymes that cleave sialic acid (also called neuraminic acid) groups from glycoproteins. Viral neuraminidase was discovered by Alfred Gottschalk (biochemist), Alfred Gottschalk at the WEHI, Walter and Eliza Hall Institute in 1957. Neuraminidase inhibitors are antiviral agents that inhibit influenza viral neuraminidase activity and are of major importance in the control of influenza. Viral neuraminidases are the members of the glycoside hydrolase family 3CAZY GH_34which comprises enzymes with only one known activity; sialidase or neuraminidase . Neuraminidases cleave the terminal sialic acid residues from carbohydrate chains in glycoproteins. Sialic acid is a negatively charged sugar associated with the protein and lipid portions of lipoproteins. To infect a host cell, the influenza virus attaches to the exteri ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycoside Hydrolase Family 34
Viral neuraminidase is a type of neuraminidase found on the surface of influenza viruses that enables the virus to be released from the host cell. Neuraminidases are enzymes that cleave sialic acid (also called neuraminic acid) groups from glycoproteins. Viral neuraminidase was discovered by Alfred Gottschalk at the Walter and Eliza Hall Institute in 1957. Neuraminidase inhibitors are antiviral agents that inhibit influenza viral neuraminidase activity and are of major importance in the control of influenza. Viral neuraminidases are the members of the glycoside hydrolase family 3CAZY GH_34which comprises enzymes with only one known activity; sialidase or neuraminidase . Neuraminidases cleave the terminal sialic acid residues from carbohydrate chains in glycoproteins. Sialic acid is a negatively charged sugar associated with the protein and lipid portions of lipoproteins. To infect a host cell, the influenza virus attaches to the exterior cell surface using hemagglu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Viral Neuraminidase
Viral neuraminidase is a type of neuraminidase found on the surface of influenza viruses that enables the virus to be released from the host cell. Neuraminidases are enzymes that cleave sialic acid (also called neuraminic acid) groups from glycoproteins. Viral neuraminidase was discovered by Alfred Gottschalk (biochemist), Alfred Gottschalk at the WEHI, Walter and Eliza Hall Institute in 1957. Neuraminidase inhibitors are antiviral agents that inhibit influenza viral neuraminidase activity and are of major importance in the control of influenza. Viral neuraminidases are the members of the glycoside hydrolase family 3CAZY GH_34which comprises enzymes with only one known activity; sialidase or neuraminidase . Neuraminidases cleave the terminal sialic acid residues from carbohydrate chains in glycoproteins. Sialic acid is a negatively charged sugar associated with the protein and lipid portions of lipoproteins. To infect a host cell, the influenza virus attaches to the exteri ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Neuraminidase Ribbon Diagram
Exo-α-sialidase (, sialidase, neuraminidase; systematic name acetylneuraminyl hydrolase) is a glycoside hydrolase that cleaves the glycosidic linkages of neuraminic acids: : Hydrolysis of α-(2→3)-, α-(2→6)-, α-(2→8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. Viral neuraminidase was the first neuraminidase to be identified. It was discovered in 1957 by Alfred Gottschalk at the Walter and Eliza Hall Institute in Melbourne. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologues are found in mammalian cells, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sialidase
Exo-α-sialidase (, sialidase, neuraminidase; systematic name acetylneuraminyl hydrolase) is a glycoside hydrolase that cleaves the glycosidic linkages of neuraminic acids: : Hydrolysis of α-(2→3)-, α-(2→6)-, α-(2→8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. Viral neuraminidase was the first neuraminidase to be identified. It was discovered in 1957 by Alfred Gottschalk at the Walter and Eliza Hall Institute in Melbourne. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologues are found in mammalian cel ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycoside Hydrolase Family 83
Hemagglutinin-neuraminidase refers to a single viral protein that has both hemagglutinin and (endo) neuraminidase activity. This is in contrast to the proteins found in influenza, where both functions exist but in two separate proteins. Its neuraminidase domain has the CAZy designation glycoside hydrolase family 83 (GH83). It does show a structural similarity to influenza viral neuraminidase and has a six-bladed beta-propeller In structural biology, a beta-propeller (β-propeller) is a type of all-β protein architecture characterized by 4 to 8 highly symmetrical blade-shaped beta sheets arranged toroidally around a central axis. Together the beta-sheets form a funnel- ... structure. This Pfam entry also matches measles hemagglutinin (cd15467), which has a "dead" neuraminidase part repurposed as a receptor binding site. Hemagglutinin-neuraminidase allows the virus to stick to a potential host cell, and cut itself loose if necessary. Hemagglutinin-neuraminidase can be found in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
NEU1
Sialidase-1, is a mammalian lysosomal neuraminidase enzyme which in humans is encoded by the ''NEU1'' gene. Function The protein SIALIDASE-1 encoded by the NEU-1 gene encodes the lysosomal enzyme SIALIDASE-1, which cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, this enzyme is part of a heterotrimeric complex together with beta-galactosidase and cathepsin A (the latter also referred to as 'protective protein'). Mutations in this gene can lead to sialidosis. Clinical significance Mutations in ''NEU1'' leads to sialidosis, a rare lysosomal storage disease Lysosomal storage diseases (LSDs; ) are a group of over 70 rare inherited metabolic disorders that result from defects in lysosomal function. Lysosomes are sacs of enzymes within cells that digest large molecules and pass the fragments on to other .... Sialidase has also been shown to enhance recovery from spinal cord contusion injury when injected in rats. Int ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Influenza
Influenza, commonly known as the flu, is an infectious disease caused by influenza viruses. Symptoms range from mild to severe and often include fever, runny nose, sore throat, muscle pain, headache, coughing, and fatigue. These symptoms begin one to four (typically two) days after exposure to the virus and last for about two to eight days. Diarrhea and vomiting can occur, particularly in children. Influenza may progress to pneumonia from the virus or a subsequent bacterial infection. Other complications include acute respiratory distress syndrome, meningitis, encephalitis, and worsening of pre-existing health problems such as asthma and cardiovascular disease. There are four types of influenza virus: types A, B, C, and D. Aquatic birds are the primary source of influenza A virus (IAV), which is also widespread in various mammals, including humans and pigs. Influenza B virus (IBV) and influenza C virus (ICV) primarily infect humans, and influenza D virus (IDV) i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alfred Gottschalk (biochemist)
Alfred Gottschalk (22 April 1894 – 4 October 1973) was a German biochemist who was a leading authority in glycoprotein research. During his career he wrote 216 research papers and reviews, and four books.Frank Fenner"Gottschalk, Alfred (1894–1973)" ''Australian Dictionary of Biography'', National Centre of Biography, Australian National University. First published in ''Australian Dictionary of Biography'', Volume 14, (MUP), 1996.Trikojus, V.M., 1974 ''Records of the Australian Academy of Science'', Vol. 3. Gottschalk was born in Aachen, the third of four children to Benjamin and Rosa Gottschalk, who had Jewish heritage. He was raised Catholic. He choose to study medicine, from 1912 he attended the Universities of Ludwig Maximilian University of Munich, Munich, University of Freiburg, Freiburg im Breisgau and University of Bonn, Bonn. During the World War I, war he served in the medical corps of the Imperial German Army, German Army. He completed his medical degree in 1920, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Neuraminic Acid
Neuraminic acid (5-amino-3,5-dideoxy-D-''glycero''-D-''galacto''-non-2-ulosonic acid) is an Sugar acid, acidic (in particular Sugar acid#ulosonic acid, ulosonic) amino sugar, amino sugar with a backbone formed by nine carbon atoms. Although 9-carbon sugars do not occur naturally, neuraminic acid may be regarded as a theoretical 9-carbon ketose in which the first link of the chain (the –CH2OH at Monosaccharide#Linear-chain monosaccharides, position 1) is Oxidation, oxidised into a carboxyl group (–C(=O)OH), the hydroxyl group at position 3 is deoxidised (oxygen is removed from it), and the hydroxyl group at position 5 is substituted with an amino group (–NH2). Neuraminic acid may also be visualized as the product of an aldol condensation, aldol-condensation of pyruvic acid and D-mannosamine (2-amino-2-deoxy-mannose). Neuraminic acid does not occur naturally, but many of its derivatives are found widely distributed in animal tissues and in bacteria, especially in glycopro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycoside Hydrolase
In biochemistry, glycoside hydrolases (also called glycosidases or glycosyl hydrolases) are a class of enzymes which catalysis, catalyze the hydrolysis of glycosidic bonds in polysaccharide, complex sugars. They are extremely common enzymes, with roles in nature including degradation of biomass such as cellulose (cellulase), hemicellulose, and starch (amylase), in anti-bacterial defense strategies (e.g., lysozyme), in pathogenesis mechanisms (e.g., viral neuraminidases) and in normal cellular function (e.g., trimming alpha-Mannosidase, mannosidases involved in N-linked glycoprotein, ''N''-linked glycoprotein biosynthesis). Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds. Occurrence and importance Glycoside hydrolases are found in essentially all domains of life. In prokaryotes, they are found both as intracellular and extracellular enzymes that are largely involved in nutrient acquisitio ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
