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Maltose (/ ˈ m ɔː l t oʊ s / [2] or / ˈ m ɔː l t oʊ z / [3]), also known as maltobiose or malt sugar, is a disaccharide formed from two units of glucose joined with an α(1→4) bond. In the isomer isomaltose , the two glucose molecules are joined with an α(1→6) bond.
Maltase-glucoamylase is an alpha-glucosidase digestive enzyme. It consists of two subunits with differing substrate specificity. Recombinant enzyme studies have shown that its N-terminal catalytic domain has highest activity against maltose, while the C-terminal domain has a broader substrate specificity and activity against glucose oligomers. [7]
Maltose Ligand (NAG) interactions in Maltase-Glucoamylase Interactions of oligosaccharides in Alpha-amylase. Maltase is an informal name for a family of enzymes that catalyze the hydrolysis of disaccharide maltose into two simple sugars of glucose. Maltases are found in plants, bacteria, yeast, humans, and other vertebrates.
Glycation (non-enzymatic glycosylation) is the covalent attachment of a sugar to a protein, lipid or nucleic acid molecule. [1] Typical sugars that participate in glycation are glucose, fructose, and their derivatives.
In enzymology, a maltose α-D-glucosyltransferase (EC 5.4.99.16) is an enzyme that catalyzes the chemical reaction maltose ⇌ {\displaystyle \rightleftharpoons } alpha,alpha-trehalose Hence, this enzyme has one substrate , maltose , and one product , alpha,alpha-trehalose .
In enzymology, a maltose synthase (EC 2.4.1.139) is an enzyme that catalyzes the chemical reaction 2 alpha-D-glucose 1-phosphate + H 2 O ⇌ {\displaystyle \rightleftharpoons } maltose + 2 phosphate Thus, the two substrates of this enzyme are alpha-D-glucose 1-phosphate and H 2 O , whereas its two products are maltose and phosphate .
Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B. Glycosyltransferases (GTFs, Gtfs) are enzymes that establish natural glycosidic linkages.They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur ...
A diastase (/ ˈ d aɪ ə s t eɪ z /; from Greek διάστασις, "separation") is any one of a group of enzymes that catalyses the breakdown of starch into maltose.For example, the diastase α-amylase degrades starch to a mixture of the disaccharide maltose; the trisaccharide maltotriose, which contains three α (1-4)-linked glucose residues; and oligosaccharides, known as dextrins, that ...
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