EC Number   |
Reference |
|---|
   3.2.1.139 | crystal structure of mutant E292A in complex with its substrate aldobiouronic acid |
665485 |
| 3.2.1.139 | hanging drop method, several high resolution crystal structures of the alpha-glucuronidase in complex with its substrate and products: structure of wild-type enzyme, structure of mutant enzyme E285N, mutant enzyme in complex with aldotetraouronic acid |
646736 |
| 3.2.1.139 | hanging-drop vapor diffusion method |
646737 |
| 3.2.1.139 | hanging-drop vapor diffusion method. Two crystal forms: T1 and M1. T1 form: space group P4(1)2(1)2 or P4(3)2(1)2 with unit-cell dimensions a = b = 76.1 A, c = 331.2 A. The crystals are mechanically strong, are stable in the X-ray beam and diffract X-rays to better than 2.4 A resolution. M1 form: space group P2(1) with unit-cell dimensions a = 65.8, b = 127.4, c = 96.6 A and beta = 97.9°. The crystals are quite strong and stable and diffract to better than 2.8 A resolution |
663511 |
| 3.2.1.139 | molecular modeling of structure. The likely catalytic residues are Asp303 (nucleophile) and Glu350 (proton donor). An arginine (Arg299 in Pjdr2) is conserved in all the Agu115 enzymes considered. The xylose-binding cleft bounded by Trp249 and Val426 in Agu115A is predicted to be lined by Trp272 and Met401 in the Agu115A model |
737522 |
| 3.2.1.139 | purified recombinant His6-tagged wild-type and selenomethionine-labeled enzyme or enzyme complexed with alpha-D-glucuronic acid, 10 mg/ml protein mixed with 19% PEG3350, 0.2 M sodium citrate, pH 5.5, soaking with 300 mM glucuronic acid for the complexed structure, use of mother liquor supplemented with 15% v/v PEG 400 or paratone N oil as cryoprotectant, X-ray diffraction structure determination and analysis at 2.14-3.0 A resolution |
732167 |
| 3.2.1.139 | sitting drop vapor diffusion method, using 20% (w/v) PEG 2000 MME and 0.1 M Tris pH 7.0 |
713669 |
| 3.2.1.139 | 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 |
738687 |
