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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.
α-Amylase is an enzyme (EC 3.2.1.1; systematic name 4-α-D-glucan glucanohydrolase) that hydrolyses α bonds of large, α-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose, through the following biochemical process: [2]
Maltose-binding protein (MBP) is a part of the maltose/maltodextrin system of Escherichia coli, which is responsible for the uptake and efficient catabolism of maltodextrins. It is a complex regulatory and transport system involving many proteins and protein complexes. MBP has an approximate molecular mass of 42.5 kilodaltons.
Amylose A is a parallel double-helix of linear chains of glucose. Amylose is made up of α(1→4) bound glucose molecules. The carbon atoms on glucose are numbered, starting at the aldehyde (C=O) carbon, so, in amylose, the 1-carbon on one glucose molecule is linked to the 4-carbon on the next glucose molecule (α(1→4) bonds). [3]
EC 6, Ligases: join two molecules with covalent bonds. EC 7, Translocases: catalyze the movement of ions or molecules across membranes, or their separation within membranes. These sections are subdivided by other features such as the substrate, products, and chemical mechanism. An enzyme is fully specified by four numerical designations.
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Hydrolysis reaction of Maltose being broken at the 1-4 alpha-glucosidase linkage. The mechanism of all FamilyGH13 enzymes is to break a α-glucosidase linkage by hydrolyzing it. Maltase focuses on breaking apart maltose, a disaccharide that is a link between 2 units of glucose, at the α-(1->4) bond.
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