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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.
These isomers are not distinguished by absolute configuration but rather by the position of substituent groups relative to a plane of reference, as across a double bond or relative to a ring structure. Cis isomers have substituent groups on the same side and trans isomers have groups on opposite sides. [2] This category is not broken down any ...
L-Ribose Fischer Projection. Ribose is a simple sugar and carbohydrate with molecular formula C 5 H 10 O 5 and the linear-form composition H−(C=O)−(CHOH) 4 −H. The naturally occurring form, d-ribose, is a component of the ribonucleotides from which RNA is built, and so this compound is necessary for coding, decoding, regulation and expression of genes.
Discounting isomers that are equivalent under rotations, there are nine isomers that differ by this criterion, and behave as different stable substances (two of them being enantiomers of each other). The most common one in nature ( myo -inositol) has the hydroxyls on carbons 1, 2, 3 and 5 on the same side of that plane, and can therefore be ...
Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.
The two domains are separated by a deep groove that contains the maltose/maltodextrin binding site. Comparison of the structures of the liganded and unliganded forms of MBP has shown that the binding of maltose induces a major conformational change that closes the groove by a rigid motion of the two domains around the linking polypeptide hinge ...
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]
Working from the non-reducing end, β-amylase catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units at a time. During the ripening of fruit, β-amylase breaks starch into maltose, resulting in the sweet flavor of ripe fruit. β-amylase is present in an inactive form prior to seed germination.