EC Number   |
General Information |
Reference |
|---|
    2.4.1.25 | physiological function |
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan |
-, 776728 |
| 2.4.1.25 | physiological function |
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Amylomaltase may be involved in the synthesis of trehalose in Corynebacterium glutamicum. The sugar is required by the bacterium to counteract osmotic stress and for the production of mycolic acids, important components of the cell envelope in Corynebacteriaceae |
-, 776728 |
| 2.4.1.25 | physiological function |
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Presence of glucoamylase-resistant glucans among the products of the reaction of the Thermus thermophilus enzyme on amylose |
-, 776728 |
| 2.4.1.25 | physiological function |
enzyme amylomaltase (AMM) from Thermus thermophilus is a thermo-active 4-alpha-glucanotransferase. It catalyzes the transfer of linear glucan segments from the donor amylose (AM) to the acceptor non-reducing end of the amylopectin (AP) chains via a disproportionation reaction. In a model starch system, AMM can in situ change starch fine molecular structure by elongating the AP chains at the expense of the length of AM chains resulting in significantly lower extent and rate of starch digestion |
777344 |
| 2.4.1.25 | physiological function |
enzyme amylomaltase has the ability to synthesize cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin |
-, 777118 |
| 2.4.1.25 | physiological function |
glycogen debranching enzyme (GDE) is bifunctional in that it exhibits both 4-alpha-glucanotransferase (EC 2.4.1.25) and amylo-alpha-1,6-glucosidase activity at two distinct catalytic sites. GDE converts the phosphorylase-limit biantennary branch into a linear maltooligosyl residue, which is then subjected to phosphorylase, and glycogen degradation continues |
771779 |
| 2.4.1.25 | physiological function |
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants |
-, 776247 |
