EC Number   |
|---|
    4.1.1.22 | - |
| 4.1.1.22 | core domain, to 1.8 A resolution. Three dimers per asymmetric unit. Molecular replacement carried out using the AroDC structure as a model |
| 4.1.1.22 | crystal structure at 3.0 A resolution |
| 4.1.1.22 | crystal structure of active HDC at pH 4.8 at 2.5 A resolution, crystal structure of less active HDC at pH 8.0 at 2.7 A resolution, crystals are grown at room temperatur by hanging-drop vapor diffusion, drops contain 0.004 ml HDC at 12.5 mg/ml, 0.001 ml n-dodecyl-beta-D-maltoside and 0.005 ml precipitant solution from the well containing 25% polyethylene glycol 400, 8% polyethylene glycol 400, 100 mM Tris pH 8.0, and 100 mM sodium acetate, enzyme activity is regulated by pH-induced structural changes |
| 4.1.1.22 | in complex with the inhibitor histidine methyl ester, to 1.8 A resolution. Cofactor pyridoxal 5'-phosphate is located in the large domain. The pyridine ring of pyridoxal 5'-phosphate is sandwiched between the methyl group of Ala275 and the imidazole ring of His194. Residue Ser354 is a key residue for substrate specificity |
| 4.1.1.22 | modeling of complex with inhibitor epigallocatechin-3-gallate. The presence of epigallocatechin-3-gallate contiguous to the active site entrance leads to the movement of several residues in the active site. Epigallocatechin-3-gallate occludes the entrance channel to the enzyme active site and establishes new interactions with residues in the active site. These residues turn outward when the active site collapses |
