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Alpha-L-fucosidase
In enzymology, an alpha-L-fucosidase () is an enzyme that catalyzes the chemical reaction :an alpha-L-fucoside + H2O \rightleftharpoons L-fucose + an alcohol Thus, the two substrates of this enzyme are alpha-L-fucoside and H2O, whereas its two products are L-fucose and alcohol. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is alpha-L-fucoside fucohydrolase. This enzyme is also called alpha-fucosidase. This enzyme participates in n-glycan degradation and glycan structures - degradation. Deficiency of this enzyme is called Fucosidosis. In CAZy, alpha-L-fucosidases are found in glycoside hydrolase family 29 and glycoside hydrolase family 95. Structural studies As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and . Human medical studies It was in a recent study by Endreffy, Bjørklund and coll ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycoside Hydrolase Family 29
In molecular biology, glycoside hydrolase family 29 is a family of glycoside hydrolases. Glycoside hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes. Glycoside hydrolase family 29 includes alpha-L-fucosidases, They are lysosomal enzymes responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Alpha-L-fucosidase is responsible for hydrolysing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Fucosylated glycoconjugates are ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fucosidosis
Fucosidosis is a rare lysosomal storage disorder in which the FUCA1 gene experiences mutations that severely reduce or stop the activity of the alpha-L-fucosidase enzyme. The result is a buildup of complex sugars in parts of the body, which leads to death. Fucosidosis is one of nine identified glycoprotein storage diseases. The gene encoding the alpha-fucosidase, FUCA 1, was found to be located to the short arm of chromosome 1p36 - p34, by Carrit and co-workers, in 1982. Cause Fucosidosis is an autosomal recessive disorder that affects many areas of the body. Mutations in the FUCA1 gene causes fucosidosis. The FUCA1 gene provides instructions for making an enzyme called alpha-L-fucosidase. The enzyme plays a role in the breakdown of complex sugars in the body. The disorder is characterized by lysosomal accumulation of a variety of glycoproteins, glycolipids, and oligosaccharides that contain fucose moieties. The deficiency of the enzyme alpha-L-fucosidase, which is used to metab ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzymology
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Families
A protein family is a group of evolutionarily related proteins. In many cases, a protein family has a corresponding gene family, in which each gene encodes a corresponding protein with a 1:1 relationship. The term "protein family" should not be confused with family as it is used in taxonomy. Proteins in a family descend from a common ancestor and typically have similar three-dimensional structures, functions, and significant sequence similarity. The most important of these is sequence similarity (usually amino-acid sequence), since it is the strictest indicator of homology and therefore the clearest indicator of common ancestry. A fairly well developed framework exists for evaluating the significance of similarity between a group of sequences using sequence alignment methods. Proteins that do not share a common ancestor are very unlikely to show statistically significant sequence similarity, making sequence alignment a powerful tool for identifying the members of protein familie ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
FUCA2
Plasma alpha-L-fucosidase (see alpha-L-fucosidase) is an enzyme that in humans is encoded by the ''FUCA2'' gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a ba .... References Further reading * * * * * * * * {{gene-6-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
1,6-alpha-L-fucosidase
In enzymology, a 1,6-alpha-L-fucosidase () is an enzyme that catalyzes the chemical reaction A chemical reaction is a process that leads to the IUPAC nomenclature for organic transformations, chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the pos ... :Hydrolysis of 1,6-linkages between alpha-L-fucose and N-acetyl-D-glucosamine in glycopeptides such as immunoglobulin G glycopeptide and fucosyl-asialo-agalacto-fetuin This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is 1,6-L-fucosyl-N-acetyl-D-glucosaminylglycopeptide fucohydrolase. This enzyme is also called alpha-L-fucosidase. References * EC 3.2.1 Enzymes of unknown structure {{3.2-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
1,3-alpha-L-fucosidase
In enzymology, a 1,3-alpha-L-fucosidase () is an enzyme that catalyzes the chemical reaction of cleaving the 1,3-linkages between alpha-L- fucose and N-acetyl glucosamine residues in glycoproteins. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is 3-alpha-L-fucosyl-N-acetylglucosaminyl-glycoprotein fucohydrolase. This enzyme is also called almond emulsin fucosidase I. This enzyme participates in the degradation of glycan The terms glycans and polysaccharides are defined by IUPAC as synonyms meaning "compounds consisting of a large number of monosaccharides linked glycosidically". However, in practice the term glycan may also be used to refer to the carbohydrate p ... structures. References * * * EC 3.2.1 Enzymes of unknown structure {{3.2-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
1,2-alpha-L-fucosidase
In enzymology, a 1,2-alpha-L-fucosidase () is an enzyme that catalyzes the chemical reaction A chemical reaction is a process that leads to the IUPAC nomenclature for organic transformations, chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the pos ... :methyl-2-alpha-L-fucopyranosyl-beta-D-galactoside + HO \rightleftharpoons L-fucose + methyl beta-D-galactoside Thus, the two substrates of this enzyme are methyl-2-alpha-L-fucopyranosyl-beta-D-galactoside and HO, whereas its two products are L-fucose and methyl beta-D-galactoside. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is 2-alpha-L-fucopyranosyl-beta-D-galactoside fucohydrolase. Other names in common use include almond emulsin fucosidase, and alpha-(1->2)-L-fucosidase. Structural studies As of late 2007 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Geir Bjørklund
Geir Bjørklund (born 20 April 1969 in Mo i Rana, Norway) is a researcher, health science writer, and scientific advisor. He has contributed to studying interactions of nutritional and environmental factors related to human physiology, biochemistry, and pathology, as well as clinical applications to pursue good health and prevent and treat disease. Research and publishing Geir Bjørklund was among the first researchers in Norway who evaluated the risk of occupational disease in dentistry due to mercury exposure. In the late 1990s, he had consulting assignments for the Norwegian Board of Health (Statens helsetilsyn). He was co-author of two of their reports on the use of dental filling materials. In 1995, Bjørklund founded Tenner & Helse, the membership magazine of Forbundet Tenner og Helse (Norwegian Dental Patient Association), and was its editor until the summer of 1999. In the 1990s, he was also a freelance journalist for ''Sunnhetsbladet'', a Norwegian health magazine. In 2 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Data Bank
The Protein Data Bank (PDB) is a database for the three-dimensional structural data of large biological molecules, such as proteins and nucleic acids. The data, typically obtained by X-ray crystallography, NMR spectroscopy, or, increasingly, cryo-electron microscopy, and submitted by biologists and biochemists from around the world, are freely accessible on the Internet via the websites of its member organisations (PDBe, PDBj, RCSB, and BMRB). The PDB is overseen by an organization called the Worldwide Protein Data Bank, wwPDB. The PDB is a key in areas of structural biology, such as structural genomics. Most major scientific journals and some funding agencies now require scientists to submit their structure data to the PDB. Many other databases use protein structures deposited in the PDB. For example, SCOP and CATH classify protein structures, while PDBsum provides a graphic overview of PDB entries using information from other sources, such as Gene ontology. History Two force ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tertiary Structure
Protein tertiary structure is the three dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure.Branden C. and Tooze J. "Introduction to Protein Structure" Garland Publishing, New York. 1990 and 1991. A number of tertiary structures may fold into a quaternary structure.Kyte, J. "Structure in Protein Chemistry." Garland Publishing, New York. 1995. History The science of the tertiary structure of proteins has progressed from one of hypothesis to one of detailed definition. Although Emil Fischer had suggested proteins were made of polypept ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycoside Hydrolase Family 95
In chemistry, a glycoside is a molecule in which a sugar is bound to another functional group via a glycosidic bond. Glycosides play numerous important roles in living organisms. Many plants store chemicals in the form of inactive glycosides. These can be activated by enzyme hydrolysis, which causes the sugar part to be broken off, making the chemical available for use. Many such plant glycosides are used as medications. Several species of '' Heliconius'' butterfly are capable of incorporating these plant compounds as a form of chemical defense against predators. In animals and humans, poisons are often bound to sugar molecules as part of their elimination from the body. In formal terms, a glycoside is any molecule in which a sugar group is bonded through its anomeric carbon to another group via a glycosidic bond. Glycosides can be linked by an O- (an ''O-glycoside''), N- (a ''glycosylamine''), S-(a ''thioglycoside''), or C- (a ''C-glycoside'') glycosidic bond. According to t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
