Galactosidases
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Galactosidases
Galactosidases are enzymes (glycoside hydrolases) that catalyze the hydrolysis of galactosides into monosaccharides. Galactosides can be classified as either alpha or beta. If the galactoside is classified as an alpha-galactoside, the enzyme is called alpha-galactosidase, and is responsible for catalyzing the hydrolysis of substrates that contain α-galactosidic residues, such as glycosphingolipids or glycoproteins. On the other hand, if it is a beta-galactoside, it is called beta-galactosidase, and is responsible for breaking down the disaccharide lactose into its monosaccharide components, glucose and galactose Both varieties of galactosidase are categorized under the EC number 3.2.1. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Lack of alpha-galactosidase activity in leukocytes has been linked to Fabry Disease. Galactosidases have a variety of uses, including the production of prebiotics Prebiotics are compoun ...
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Agalsidase Beta
α-Galactosidase ( EC 3.2.1.22, α-GAL, α-GAL A; systematic name α-D-galactoside galactohydrolase) is a glycoside hydrolase enzyme that catalyses the following reaction: : Hydrolysis of terminal, non-reducing α-D-galactose residues in α-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids It catalyzes many catabolic processes, including cleavage of glycoproteins, glycolipids, and polysaccharides. The enzyme is encoded by the ''GLA'' gene. Two recombinant forms of human α-galactosidase are called agalsidase α (INN) and agalsidase β (INN). A mold-derived form is the primary ingredient in gas relief supplements. Function This enzyme is a homodimeric glycoprotein that hydrolyses the terminal α-galactosyl moieties from glycolipids and glycoproteins. It predominantly hydrolyzes ceramide trihexoside, and it can catalyze the hydrolysis of melibiose into galactose and glucose. Reaction mechanism Disease relevance Fabry disease ...
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Galactosides
A galactoside is a glycoside containing galactose. The H of the OH group on carbon-1 of galactose is replaced by an organic moiety. Depending on whether the glycosidic bond lies "above" or "below" the plane of the galactose molecule, galactosides are classified as α-galactosides or β-galactosides. A β-galactoside is a type of galactoside in which the glycosidic bond lies above the plane of the galactose Galactose (, '' galacto-'' + ''-ose'', "milk sugar"), sometimes abbreviated Gal, is a monosaccharide sugar that is about as sweet as glucose, and about 65% as sweet as sucrose. It is an aldohexose and a C-4 epimer of glucose. A galactose molecu ... residue. The most commonly recognized and used β-galactoside in biochemistry is lactose. However, other chemicals, such as ONPG, are known, but these are typically synthesized for biochemical assays. Galactosides play significant roles in metabolic processes of many organisms and are hydrolyzed by a class of enzymes called g ...
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Alpha-galactosidase
α-Galactosidase ( EC 3.2.1.22, α-GAL, α-GAL A; systematic name α-D-galactoside galactohydrolase) is a glycoside hydrolase enzyme that catalyses the following reaction: : Hydrolysis of terminal, non-reducing α-D-galactose residues in α-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids It catalyzes many catabolic processes, including cleavage of glycoproteins, glycolipids, and polysaccharides. The enzyme is encoded by the ''GLA'' gene. Two recombinant forms of human α-galactosidase are called agalsidase α (INN) and agalsidase β (INN). A mold-derived form is the primary ingredient in gas relief supplements. Function This enzyme is a homodimeric glycoprotein that hydrolyses the terminal α-galactosyl moieties from glycolipids and glycoproteins. It predominantly hydrolyzes ceramide trihexoside, and it can catalyze the hydrolysis of melibiose into galactose and glucose. Reaction mechanism Disease relevance Fabry disease ...
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Agalsidase Alfa
α-Galactosidase ( EC 3.2.1.22, α-GAL, α-GAL A; systematic name α-D-galactoside galactohydrolase) is a glycoside hydrolase enzyme that catalyses the following reaction: : Hydrolysis of terminal, non-reducing α-D-galactose residues in α-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids It catalyzes many catabolic processes, including cleavage of glycoproteins, glycolipids, and polysaccharides. The enzyme is encoded by the ''GLA'' gene. Two recombinant forms of human α-galactosidase are called agalsidase α (INN) and agalsidase β (INN). A mold-derived form is the primary ingredient in gas relief supplements. Function This enzyme is a homodimeric glycoprotein that hydrolyses the terminal α-galactosyl moieties from glycolipids and glycoproteins. It predominantly hydrolyzes ceramide trihexoside, and it can catalyze the hydrolysis of melibiose into galactose and glucose. Reaction mechanism Disease relevance Fabry disease ...
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Beta-galactosidase
β-Galactosidase (EC 3.2.1.23, lactase, beta-gal or β-gal; systematic name β-D-galactoside galactohydrolase), is a glycoside hydrolase enzyme that catalyzes hydrolysis of terminal non-reducing β-D-galactose residues in β-D-galactosides. β-Galactosides include carbohydrates containing galactose where the glycosidic bond lies above the galactose molecule. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Function β-Galactosidase is an exoglycosidase which hydrolyzes the β-glycosidic bond formed between a galactose and its organic moiety. It may also cleave fucosides and arabinosides but with much lower efficiency. It is an essential enzyme in the human body. Deficiencies in the protein can result in galactosialidosis or Morquio B syndrome. In '' E. coli'', the ''lacZ'' gene is the structural gene for β-galactosidase; which is present as part of the inducible system ''lac'' operon which is activ ...
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Enzymes
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different molecules known as product (chemistry), products. Almost all metabolism, metabolic processes in the cell (biology), 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, 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 Ribozyme, catalytic RNA molecules, called ribozymes. Enzymes' Chemical specificity, specific ...
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Galactose
Galactose (, '' galacto-'' + '' -ose'', "milk sugar"), sometimes abbreviated Gal, is a monosaccharide sugar that is about as sweet as glucose, and about 65% as sweet as sucrose. It is an aldohexose and a C-4 epimer of glucose. A galactose molecule linked with a glucose molecule forms a lactose molecule. Galactan is a polymeric form of galactose found in hemicellulose, and forming the core of the galactans, a class of natural polymeric carbohydrates. D-Galactose is also known as brain sugar since it is a component of glycoproteins (oligosaccharide-protein compounds) found in Nerve tissue, nerve tissue. Etymology The word ''galactose'' was coined by Charles Weissman in the mid-19th century and is derived from Greek ''galaktos'' (of milk) and the generic chemical suffix for sugars ''-ose''. The etymology is comparable to that of the word '' lactose'' in that both contain roots meaning "milk sugar". Lactose is a disaccharide of galactose plus glucose. Structure and isomerism Gal ...
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Fabry Disease
Fabry disease, also known as Anderson–Fabry disease, is a rare genetic disease that can affect many parts of the body, including the kidneys, heart, and skin. Fabry disease is one of a group of conditions known as lysosomal storage diseases. The genetic mutation that causes Fabry disease interferes with the function of an enzyme that processes biomolecules known as sphingolipids, leading to these substances building up in the walls of blood vessels and other organs. It is inherited in an X-linked manner. Fabry disease is sometimes diagnosed using a blood test that measures the activity of the affected enzyme called alpha-galactosidase, but genetic testing is also sometimes used, particularly in females. The treatment for Fabry disease varies depending on the organs affected by the condition, and the underlying cause can be addressed by replacing the enzyme that is lacking. The first descriptions of the condition were made simultaneously by dermatologist Johannes Fabry and ...
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Recombinant DNA
Recombinant DNA (rDNA) molecules are DNA molecules formed by laboratory methods of genetic recombination (such as molecular cloning) that bring together genetic material from multiple sources, creating sequences that would not otherwise be found in the genome. Recombinant DNA is the general name for a piece of DNA that has been created by combining at least two fragments from two different sources. Recombinant DNA is possible because DNA molecules from all organisms share the same chemical structure, and differ only in the nucleotide sequence within that identical overall structure. Recombinant DNA molecules are sometimes called chimeric DNA, because they can be made of material from two different species, like the mythical chimera. R-DNA technology uses palindromic sequences and leads to the production of sticky and blunt ends. The DNA sequences used in the construction of recombinant DNA molecules can originate from any species. For example, plant DNA may be joined to bacter ...
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Enzyme Commission Number
The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the corresponding enzyme-catalyzed reaction. EC numbers do not specify enzymes but enzyme-catalyzed reactions. If different enzymes (for instance from different organisms) catalyze the same reaction, then they receive the same EC number. Furthermore, through convergent evolution, completely different protein folds can catalyze an identical reaction (these are sometimes called non-homologous isofunctional enzymes) and therefore would be assigned the same EC number. By contrast, UniProt identifiers uniquely specify a protein by its amino acid sequence. Format of number Every enzyme code consists of the letters "EC" followed by four numbers separated by periods. Those numbers represent a progressively finer classification of the enzyme. Preliminary EC ...
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Lactose
Lactose is a disaccharide sugar synthesized by galactose and glucose subunits and has the molecular formula C12H22O11. Lactose makes up around 2–8% of milk (by mass). The name comes from ' (gen. '), the Latin word for milk, plus the suffix '' -ose'' used to name sugars. The compound is a white, water-soluble, non-hygroscopic solid with a mildly sweet taste. It is used in the food industry. Structure and reactions Lactose is a disaccharide derived from the condensation of galactose and glucose, which form a β-1→4 glycosidic linkage. Its systematic name is β-D-galactopyranosyl-(1→4)-D-glucose. The glucose can be in either the α-pyranose form or the β-pyranose form, whereas the galactose can only have the β-pyranose form: hence α-lactose and β-lactose refer to the anomeric form of the glucopyranose ring alone. Detection reactions for lactose are the Woehlk- and Fearon's test. Both can be easily used in school experiments to visualise the different lactose content o ...
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