EC Number   |
General Information |
Reference |
|---|
    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 | metabolism |
key enzymes in the pathway for maltose catabolism. Glucose derived from the action of 4-alpha-glucanotransferase is subsequently metabolized via an Embden-Meyerhof pathway |
748071 |
| 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 |
| 2.4.1.25 | more |
MQ-01 fails to exhibit mutagenic activity and does not display clastogenic properties in Chinese hamster lung fibroblast cells. In a 13-week subchronic toxicity study in rats, oral administration of MQ-01 at doses of up to 15 ml/kg body weight/day do not produce compound-related clinical signs or toxicity, changes in body weight gain, food consumption, hematology, clinical chemistry, urinalysis, organ weights, or in any gross and microscopic findings, overview |
706686 |
| 2.4.1.25 | more |
the amylomaltase from Corynebacterium glutamicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview |
-, 776247 |
| 2.4.1.25 | more |
the amylomaltase from Escherichia coli, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Residue Tyr108 may be involved in alpha-glucan binding. Molecular docking, overview |
-, 776247 |
| 2.4.1.25 | more |
the amylomaltase from Kushneria marisflavi, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview |
776247 |
| 2.4.1.25 | more |
the amylomaltase from Pelotomaculum thermopropionicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview |
-, 776247 |
| 2.4.1.25 | more |
the catalytic triad residues of TaAM consist of D293, E340, and D395 as a nucleophile, acid-base catalyst, and transition state-stabilizer, respectively. Structure-function analysis, overview |
-, 778609 |
| 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 |
