EC Number   |
|---|
   3.4.13.20 | active-site modeling of DmpA. Based on the crystal structure and the catalytic mechanism proposed for DmpA, carnosine is manually introduced into the active site of the enzyme. The model shows that carnosine fits excellently, in line with the high specific activity for this substrate |
| 3.4.13.20 | complexed with bestatin together with Zn2+, hanging drop vapour diffusion method, using 20% polyethylene glycol 3350 and 0.2 M potassium fluoride |
| 3.4.13.20 | crystal structure of the enzyme determined to 1.82 A resolution using the multiple isomorphous replacement method. The heterodimer folds into a single domain organised as an alphabetabetaalpha sandwich in which two mixed beta sheets are flanked on both sides by two alpha helices |
| 3.4.13.20 | hangig-drop vapor-diffusion method. Two crystal forms are obtained at 21°C in 13-16% PEG 2000 monomethylether at pH 9.0, adding either 0.2 M magnesium chloride or 1 M lithium chloride. Crystals of the first form belong to the space group C222(1) and diffract to 3.0 A resolution. Crystals of the second form belong to the space group P2(1)2(1)2 and diffract to 2.3 A resolution |
