Α-L-fucosidase
   HOME





Α-L-fucosidase
The enzyme α-L-fucosidase () catalyzes the following chemical reaction: an α-L-fucoside + H2O \rightleftharpoons L-fucose + an 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 α-L-fucoside fucohydrolase. This enzyme is also called α-fucosidase. It participates in ''N''-glycan degradation and glycan structure degradation. Deficiency of this enzyme is called fucosidosis. In CAZy, α-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 collaborators (2017) found an association between the activity of α-L-fucosidase-1 (FUCA-1) and chronic autoimmune disorders in children.Endreffy I, Bjørklund G, S ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

Catalysis
Catalysis () is the increase in rate of a chemical reaction due to an added substance known as a catalyst (). Catalysts are not consumed by the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recycles quickly, very small amounts of catalyst often suffice; mixing, surface area, and temperature are important factors in reaction rate. Catalysts generally react with one or more reactants to form intermediates that subsequently give the final reaction product, in the process of regenerating the catalyst. The rate increase occurs because the catalyst allows the reaction to occur by an alternative mechanism which may be much faster than the noncatalyzed mechanism. However the noncatalyzed mechanism does remain possible, so that the total rate (catalyzed plus noncatalyzed) can only increase in the presence of the catalyst and never decrease. Catalysis may be classified as either homogeneous, whose components are dispersed in the same phase (usual ...
[...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. One of Bjørklund's primary research interests is autism spectrum disorder (ASD). His work explores the potential role of metal(loid)s such as mercury, along with other environmental toxins, in the development of ASD. However, according to current knowledge, ASD is associated with genetic ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

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. Sequence similarity (usually amino-acid sequence) is one of the most common indicators of homology, or common evolutionary ancestry. Some frameworks for evaluating the significance of similarity between sequences use sequence alignment methods. Proteins that do not share a common ancestor are unlikely to show statistically significant sequence similarity, making sequence alignment a powerful tool for identifying the members of protein families. Families are sometimes grouped together into larger clades called superfamilies based on stru ...
[...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. See also * Tissue alpha-L-fucosidase Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the ''FUCA1'' gene. Alpha-fucosidase is an enzyme that breaks out fucose.HPRD entr Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fu ..., encoded by ''FUCA1'' gene References Further reading

* * * * * * * * {{gene-6-stub ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


FUCA1
Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the ''FUCA1'' gene. Alpha-fucosidase is an enzyme that breaks out fucose.HPRD entr Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. Different phenotypes include clinical features such as neurologic deterioration, growth retardation, visceromegaly, and seizures in a severe early form; coarse facial features, angiokeratoma corporis diffusum, spasticity and delayed psychomotor development in a longer surviving form; and an unusual spondylometaphyseoepiphyseal dysplasia in yet another form. upplied by OMIMref name="entrez" /> See also * FUCA2 * 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 lea ... References ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  




1,6-alpha-L-fucosidase
The enzyme 1,6-α-L-fucosidase () catalyses the following chemical reaction :Hydrolysis of 1,6-linkages between α-L-fucose and ''N''-acetyl-D-glucosamine in glycopeptides such as immunoglobulin G glycopeptide and fucosyl-asialo-agalacto-fetuin It belongs to the family of hydrolases, specifically those glycosidases that hydrolyse ''O''- and ''S''-glycosyl compounds. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ... is 1,6-L-fucosyl-''N''-acetyl-D-glucosaminylglycopeptide fucohydrolase. It is also called α-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
The enzyme 1,3-α-L-fucosidase () catalyzes the hydrolytic cleavage of the 1,3-linkages between α-L-fucose and ''N''-acetylglucosamine residues in glycoproteins. It 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-α-L-fucosyl-''N''-acetylglucosaminyl-glycoprotein fucohydrolase. This enzyme is also called almond emulsin fucosidase I. It 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 ... 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
Onekama ( ) is a village in Manistee County in the U.S. state of Michigan. The population was 399 at the 2020 census. The village is located on the northeast shore of Portage Lake and is surrounded by Onekama Township. The town's name is derived from ''Ona-ga-maa'', an Anishinaabe word which means "singing water". History The predecessor of the village of Onekama was the settlement of Portage at Portage Point, first established in 1845, at the western end of Portage Lake, at the outlet of Portage Creek. In 1871, when landowners around the land-locked lake became exasperated with the practices of the Portage Sawmill, they took the solution into their own hands and dug a channel through the narrow isthmus, opening a waterway that lowered the lake by and brought it to the same level as Lake Michigan. When this action dried out Portage Creek on May 14, 1871, the settlement, which had only the week before been designated as "Onekama" with a post office under that name, moved to th ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

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, which is overseen by the Worldwide Protein Data Bank (wwPDB). This structural data is obtained and deposited by biologists and biochemists worldwide through the use of experimental methodologies such as X-ray crystallography, Nuclear magnetic resonance spectroscopy of proteins, NMR spectroscopy, and, increasingly, cryo-electron microscopy. All submitted data are reviewed by expert Biocuration, biocurators and, once approved, are made freely available on the Internet under the CC0 Public Domain Dedication. Global access to the data is provided by the websites of the wwPDB member organizations (PDBe, PDBj, RCSB PDB, and BMRB). 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 ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

Chemical Reaction
A chemical reaction is a process that leads to the chemistry, chemical transformation of one set of chemical substances to another. When chemical reactions occur, the atoms are rearranged and the reaction is accompanied by an Gibbs free energy, energy change as new products are generated. Classically, chemical reactions encompass changes that only involve the positions of electrons in the forming and breaking of chemical bonds between atoms, with no change to the Atomic nucleus, nuclei (no change to the elements present), and can often be described by a chemical equation. Nuclear chemistry is a sub-discipline of chemistry that involves the chemical reactions of unstable and radioactive Chemical element, elements where both electronic and nuclear changes can occur. The substance (or substances) initially involved in a chemical reaction are called reagent, reactants or reagents. Chemical reactions are usually characterized by a chemical change, and they yield one or more Product (c ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

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 and the backbone 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. A number of these structures may bind to each other, forming a quaternary structure. 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 polypeptide chains and amino acid side chains, it was Dorothy Maud Wrinch who incorporated geometry into the prediction of protein structures. Wrinch demon ...
[...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 in ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]