EC Number   |
|---|
    3.2.1.3 | - |
| 3.2.1.3 | apoenzyme and enzyme complexed with acarbose, X-ray diffraction structure determination and anaylsis at 2.0 A and 1.9 A resolution, respectively |
| 3.2.1.3 | cross linked glucoamylase crystals, glucoamylase is crystallized by the batch method using ammonium sulfate as precipitant, 65% saturation, along with 20% 2-propanol as cosolvent in 500 mM acetate buffer, pH 4.5, the solution is stirred at 4°C for 30 min and then kept for 16 h at the same temperature |
| 3.2.1.3 | crystal structure of glucoamylase at 2.2-2.4 A resolution |
| 3.2.1.3 | glucoamylase I and II |
| 3.2.1.3 | in complex with alpha-(1,6)-linked isomaltotriose and isomaltotetraose at 1.2 and 1.3 A resolution, respectively. Site II binding is observed in both complexes, while site I binding is only found in the isomaltotetraose complex. Hence, site II acts as the recognition binding site for carbohydrate and site I accommodates site II to bind isomaltotetraose. Site I participates in sugar binding only when the number of glucosyl units of oligosaccharides is more than three |
| 3.2.1.3 | modeling of structure based on PDB entry 2vn7 |
| 3.2.1.3 | purified isolated N-terminal catalytic domain of the G1 isoform, generated by subtilisin cleavage, sitting-drop vapour-diffusion method, 20 mg/ml protein at pH 8.5, 22°C room temperatur, the reservoir solution contains 50 mM Tris acetate, pH 8.5, 22.5% PEG 6000, 0.4 M sodium acetate and 10% glycerol, mixing of 0.001 ml protein and reservoir solution and equilibration against 1 ml reservoir solution, 2 weeks, X-ray diffraction structure determination and analysis at 1.9 A resolution, the active site of the enzyme is in complex with both Tris and glycerol molecules, structure modelling |
| 3.2.1.3 | purified recombinant enzyme, hanging drop vapour diffusion method, 20°C, 0.0015 ml of 20 mg/ml enzyme solution is mixed with 0.0015 ml of reservoir solution containing 10% w/v PEG 5000 monomethyl ether, 186 mM D-glucose, 10 mM DTT, and 1.0 M lithium chloride, in 100 mM MES, pH 6.1, cryoprotection by 20% w/v PEG 6000, 20% v/v 2-methyl-2,4-pentanediol, 2.5 mM CaCl2, 40 mM MES, pH 6.1, X-ray diffraction structure determination and analysis at 3.3 A resolution |
| 3.2.1.3 | purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 150 nl of 18 mg/ml protein in 25 mM piperazine, pH 5.0, and 150 mM NaCl, with 150 nl of reservoir solution containing 0.1 M HEPES, pH 7.5, and 25% PEG 3350, 20°C, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement using the catalytic domain of Aspergillus awamori glucoamylase as a search model (PDB entry 1glm) |
