EC Number   |
Reference |
|---|
    2.4.1.18 | - |
636943 |
| 2.4.1.18 | crystal structure of full-length protein at 2.33 A resolution. The enzyme contains four domains: N1 beta-sandwich, N2 beta-sandwich, a central (beta/alpha)8 domain that houses the catalytic site, and a C-terminal beta-sandwich. The N1 beta-sandwich, which is formed by the first 105 amino acids and superimposes well with the N2 beta-sandwich, has an influence in substrate binding in the amylase assay |
719870 |
| 2.4.1.18 | crystal structures of truncated branching enzyme mutant DELTA112 in complex with linear oligosaccharides maltoheptaose and maltohexaose, X-ray diffraction structure determination and analysis |
735689 |
| 2.4.1.18 | determination of the crystal structure of branching enzyme I at a resolution of 1.9 A by molecular replacement using the Escherichia coli glycogen branching enzyme as a search model. Branching enzyme I is roughly ellipsoidal in shape with two globular domains that form a prominent groove proposed to serve as the alphha-polyglucan-binding site. Amino acid residues Asp344 and Glu399, postulated to play an essential role in catalysis, are located at a central cleft in the groove |
719564 |
| 2.4.1.18 | hanging drop method, active N-terminally truncated form missing the first 107 amino acids |
636953 |
| 2.4.1.18 | in the native state and in complex with glucose and substrate mimetics, to 2.4 A, 2.9 A, and 1.9 A resolution, respectively. The structure encompasses a distorted (beta/alpha)7-barrel juxtaposed to a C-terminal alpha-helical domain, which also participates in the formation of the active-site cleft. The active site comprises two acidic catalytic residues, Glu183 and Asp354, the polarizer His10, aromatic gate-keepers Trp28, Trp270, Trp407, and Trp416 and the residue Tyr233, which is fully conserved among GH13- and GH57-type branching enzymes |
721012 |
| 2.4.1.18 | mutant E399Q in complex with maltopentaose at a resolution of 2.2 A. Maltopentaose binds to a hydrophobic pocket formed by the N-terminal helix, carbohydrate-binding module 48, and alpha-amylase domain. In addition, glucose moieties can be observed at molecular surfaces on the N-terminal helix alpha2 and carbohydrate-binding module 48 |
718762 |
| 2.4.1.18 | sitting drop method, 20°C |
702734 |
| 2.4.1.18 | sitting-drop vapor-diffusion method, pH 9.3, crystals belong to P2(1) space group |
744241 |
