EC Number   |
General Information |
Reference  |
|---|
    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 | 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 | 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 |
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 | evolution |
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview |
-, 776247 |
| 2.4.1.25 | evolution |
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups. sequence comparisons, overview |
-, 776247 |
| 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 |
