EC Number   |
|---|
   3.2.1.131 | hanging drop method at 20°C, 10 mg/ml enzyme solution mixed with an equal volume of reservoir solution, containing 14% w/v polyethylene glycol 4000, 12% v/v isopropyl alcohol and 0.1 M sodium citrate, pH 5.5, tetragonal space group P41212 with a and b: 74.6 A and c: 330.3 A |
| 3.2.1.131 | sitting drop vapor diffusion method, using 16% (w/v) PEG 2000 MME and 0.1 M Tris pH 7.0 |
| 3.2.1.131 | structural analysis. Residue E288 acts at the catalytic proton donor, D367 and E395 are likely nucleophilic bases |
| 3.2.1.131 | structure reveals a five-domain architecture, with an additional insertion C+ domain that has significant impact on the domain arrangement of the protein monomer and its dimerization. The participation of domain C+ in substrate binding is supported by reduced substrate inhibition upon introducing W773A, W689A, and F696A substitutions within this domain. In addition to Asp335, residue Glu216 is essential for the catalytic activtiy |
| 3.2.1.131 | two crystal forms, form T1 is obtained by the vapour-diffusion method using polyethylene glycol as precipitant and 2-propanol as organic additive, tetragonal space group P41212 or P43212 with a and b: 76.1 A and c: 331.2 A, form M1 at slightly lower pH and lower concentration of 2-propanol, monoclinic space group P21 with a: 65.8 A, b: 127.4 A, c: 96.6 A and beta: 97.9° |
| 3.2.1.131 | using 19% (w/v) PEG3350, 0.2 M sodium citrate, pH 5.5 |
| 3.2.1.131 | vapor phase diffusion using the hanging drop method, 250 mM MgCl2 and 20% v/v ethylene glycol with 15% w/v polyethylene glycol 3350 as prcipitant at 20°C, triclinic space group P1 with a: 69.9 A, b: 74.7 A, c: 87.6 A, alpha: 115.2°, beta: 93.1° and gamma: 109.3° |
