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Glycosyl Hydrolase Family 1
Glycoside hydrolase family 1 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 CAZY GH_1comprises enzymes with a number of known activities; beta-glucosidase (); beta-galactosidase (); 6-phospho-beta-galactosidase (); 6-phospho-beta-glucosidase (); lactase-phlorizin hydrolase (), lactase (); beta-mannosidase (); myrosinase (). Subfamilies * 6-phospho-beta-galactosidase Human proteins containing this domain GBA3; KL; KLB KLB is a pop band from Brazil. The band consists of three brothers from S ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Family
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 (biology), family as it is used in taxonomy. Proteins in a family descend from a common ancestor and typically have similar protein structure, three-dimensional structures, functions, and significant Sequence homology, 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 powerf ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Beta-mannosidase
Beta-mannosidase (, ''mannanase'', ''mannase'', ''beta-D-mannosidase'', ''beta-mannoside mannohydrolase'', ''exo-beta-D-mannanase'', ''lysosomal beta A mannosidase'') is an enzyme with List of enzymes, systematic name ''beta-D-mannoside mannohydrolase'', which is in humans encoded by the ''MANBA'' gene. This enzyme catalysis, catalyses the following chemical reaction : Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides This gene encodes a member of the glycosyl hydrolase 2 family. The encoded protein localizes to the lysosome where it is the final exoglycosidase in the pathway for N-linked glycoprotein oligosaccharide catabolism. Mutations in this gene are associated with beta-mannosidosis, a lysosomal storage disease that has a wide spectrum of neurological involvement. References Further reading * * * * * * * * * * * * * * * * * * * External links * * EC 3.2.1 {{gene-4-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peripheral Membrane Proteins
Peripheral membrane proteins, or extrinsic membrane proteins, are membrane proteins that adhere only temporarily to the biological membrane with which they are associated. These proteins attach to integral membrane proteins, or penetrate the peripheral regions of the lipid bilayer. The regulatory protein subunits of many ion channels and transmembrane receptors, for example, may be defined as peripheral membrane proteins. In contrast to integral membrane proteins, peripheral membrane proteins tend to collect in the water-soluble component, or fraction, of all the proteins extracted during a protein purification procedure. Proteins with GPI anchors are an exception to this rule and can have purification properties similar to those of integral membrane proteins. The reversible attachment of proteins to biological membranes has shown to regulate cell signaling and many other important cellular events, through a variety of mechanisms. For example, the close association between many enzy ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
LCTL
Lactase-like is a protein that in humans is encoded by the LCTL gene. Lactase-like is a glycosidase enzyme. Function This gene encodes a member of family 1 glycosidases. Glycosidases are enzymes that hydrolyze glycosidic bonds and are classified into families based on primary amino acid sequence. Most members of family 1 have two conserved glutamic acid residues, which are required for enzymatic activity. The mouse ortholog of this protein has been characterized and has a domain structure of an N-terminal signal peptide, glycosidase domain, transmembrane domain, and a short cytoplasmic tail. It lacks one of the conserved glutamic acid residues important for catalysis, and its function remains to be determined (PMID: 12084582). Alternative splicing results in multiple transcript variant Alternative splicing, or alternative RNA splicing, or differential splicing, is an alternative splicing process during gene expression that allows a single gene to code for multiple proteins. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lactase
Lactase is an enzyme produced by many organisms. It is located in the brush border of the small intestine of humans and other mammals. Lactase is essential to the complete digestion of whole milk; it breaks down lactose, a sugar which gives milk its sweetness. People who have deficiency of lactase, and consume dairy products, may experience the symptoms of lactose intolerance. Lactase can be purchased as a food supplement, and is added to milk to produce "lactose-free" milk products. Lactase (also known as lactase-phlorizin hydrolase, or LPH), a part of the β-galactosidase family of enzymes, is a glycoside hydrolase involved in the hydrolysis of the disaccharide lactose into constituent galactose and glucose monomers. Lactase is present predominantly along the brush border membrane of the differentiated enterocytes lining the villi of the small intestine. In humans, lactase is encoded by the LCT gene on chromosome 2. Uses Food use Lactase is an enzyme that some people are ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
KLB (gene)
KLB is a pop band from Brazil. The band consists of three brothers from São Paulo São Paulo (, ; Portuguese for 'Saint Paul') is the most populous city in Brazil, and is the capital of the state of São Paulo, the most populous and wealthiest Brazilian state, located in the country's Southeast Region. Listed by the GaWC a ...: Kiko (Franco Finato Scornavacca), Leandro Finato Scornavacca and Bruno Finato Scornavacca. KLB stands for each brother's name. Music career The brothers began their career in 1996, with a group named "The Fenders" and after "Neon" and was composed by the three brothers and the pop singers Wanessa Camargo and Camila, who left the group. KLB started in 2000 when for the first time, the brothers Kiko, Leandro and Bruno, performed at Anhembi, São Paulo, in an award, contemplating their father Franco Scornavacca, who was receiving the "Best Brazilian Manager of the 90s. Their first single " A Dor Desse Amor" charted #1 in Brazil. The KLB phenomenon ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
KL (gene)
Klotho is an enzyme that in humans is encoded by the ''KL'' gene. There are three subfamilies of klotho: α-klotho, β-klotho, and γ-klotho. α-klotho activates FGF23, and β-klotho activates FGF19 and FGF21. When the subfamily is not specified, the word "klotho" often means the α-klotho subfamily, because α-klotho was discovered before the other subfamily members. α-klotho is highly expressed in the brain, liver and kidney. β-klotho is predominantly expressed in the liver. γ-klotho is expressed in the skin. Klotho can exist in a membrane-bound form or a (hormonal) soluble, circulating form. Proteases can convert the membrane-bound form into the circulating form. The ''KL'' gene encodes a type-I single-pass transmembrane protein that is related to β-glucuronidases. Reduced production of this protein has been observed in patients with chronic kidney failure (CKF), and this may be one of the factors underlying the degenerative processes (e.g., arteriosclerosis, osteoporosi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
GBA3
Cytosolic beta-glucosidase, also known as cytosolic beta-glucosidase-like protein 1, is a beta-glucosidase () enzyme that in humans is encoded by the ''GBA3'' gene. Function Cytosolic beta-glucosidase is a predominantly liver enzyme that efficiently hydrolyzes beta-D-glucoside and beta-D-galactoside, but not any known physiologic beta-glycoside, suggesting that it may be involved in detoxification of plant glycosides. GBA3 also has significant neutral glycosylceramidase activity (), suggesting that it may be involved in a non-lysosomal catabolic pathway of glucosylceramide metabolism. See also * Closely related enzymes ** GBA: acid β-glucosidase, ** GBA2 ''GBA2'' is the gene that encodes the enzyme non-lysosomal glucosylceramidase in humans. It has glucosylceramidase () activity. Function This gene encodes a microsomal beta-glucosidase that catalyzes the hydrolysis of bile acid 3-O-glucosides ...: acid β-glucosidase (bile acid), also References Further reading ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Myrosinase
Myrosinase (, ''thioglucoside glucohydrolase'', ''sinigrinase'', and ''sinigrase'') is a family of enzymes involved in plant defense against herbivores, specifically the mustard oil bomb. The three-dimensional structure has been elucidated and is available in the PDB (see links in the infobox). A member of the glycoside hydrolase family, myrosinase possesses several similarities with the more ubiquitous O-glycosidases. However, myrosinase is the only known enzyme found in nature that can cleave a thio-linked glucose. Its known biological function is to catalyze the hydrolysis of a class of compounds called glucosinolates. Myrosinase activity Myrosinase is regarded as a defense-related enzyme and is capable of hydrolyzing glucosinolates into various compounds, some of which are toxic. Mechanism Myrosinase catalyzes the chemical reaction :a thioglucoside + H2O \rightleftharpoons a sugar + a thiol Thus, the two substrates of this enzyme are thioglucoside and H2O, whereas it ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lactase
Lactase is an enzyme produced by many organisms. It is located in the brush border of the small intestine of humans and other mammals. Lactase is essential to the complete digestion of whole milk; it breaks down lactose, a sugar which gives milk its sweetness. People who have deficiency of lactase, and consume dairy products, may experience the symptoms of lactose intolerance. Lactase can be purchased as a food supplement, and is added to milk to produce "lactose-free" milk products. Lactase (also known as lactase-phlorizin hydrolase, or LPH), a part of the β-galactosidase family of enzymes, is a glycoside hydrolase involved in the hydrolysis of the disaccharide lactose into constituent galactose and glucose monomers. Lactase is present predominantly along the brush border membrane of the differentiated enterocytes lining the villi of the small intestine. In humans, lactase is encoded by the LCT gene on chromosome 2. Uses Food use Lactase is an enzyme that some people are ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycoside Hydrolase
Glycoside hydrolases (also called glycosidases or glycosyl hydrolases) catalyze the hydrolysis of glycosidic bonds in 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 mannosidases involved in 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 acquisition. One of the important occurrences of glycoside hydrolases in bacteria is the enzyme beta-galactosidase (LacZ), which i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
