EC Number   |
General Information |
Reference |
|---|
    2.4.1.25 | physiological function |
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes |
-, 778609 |
| 2.4.1.25 | metabolism |
a distinct macroscopic debranching pathway is proposed: via 4-alpha-glucanotransferase, the G3-residue of the donor branch is transferred to a long (n >/= 5) linear Gn-residue linked to a different branching G residue |
771779 |
| 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 | metabolism |
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism |
-, 776728 |
| 2.4.1.25 | metabolism |
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism, involvement of amylomaltase in the degradation of glycogen in Escherichia coli |
-, 776728 |
| 2.4.1.25 | metabolism |
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. Amylomaltase may be involved in the synthesis of trehalose |
-, 776728 |
| 2.4.1.25 | metabolism |
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. In Aquifex aeolicus, the enzyme might be involved in the metabolism of glycogen, since its gene is located in the glycogen operon and the bacterium lacks the gene for the maltose transport proteins |
776728 |
| 2.4.1.25 | more |
analysis of the functional amino acid positions of Corynebacterium glutamicum amylomaltase (CgAM) involved in LR-CD synthesis, overview. Molecular interactions analysis using the three-dimensional crystal structure of enzyme CgAM (PDB ID 5B68), computational analysis |
-, 777118 |
