EC Number   |
|---|
    2.5.1.54 | - |
| 2.5.1.54 | crystals grown in presence of phosphoenolpyruvate and Cd2+, soaked with erythrose 4-phosphate |
| 2.5.1.54 | hanging-drop vapor diffusion, ctystal structure of wild-type enzyme and mutant enzyme I181D |
| 2.5.1.54 | in complex with a manganese ion and phosphoenolpyruvate. Crystals contain a tetramer in the asymmetric unit. A water molecule occupies the presumed binding site for the phosphate group of 4-erythrose 4-phosphate |
| 2.5.1.54 | in complex with chorismate mutase, hanging-drop method, in 20 mM BTP, pH 7.5, 150 mM NaCl, 0.5 mM tris(2-carboxyethyl)phosphine hydrochloride, 0.2 mM phosphoenolpyruvate and 0.1 mM MnCl2, crystallization after 2 months with no ammonium sulfate and 0.1 M Tris-HCl, pH 7.9-8.0 and PEG 400 or glycerol |
| 2.5.1.54 | in complex with chorismate mutase, streak-seeding conditions in 20 mM BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane), pH 7.5, 150 mM NaCl, 0.5 mM TCEP [tris(2-carboxyethyl)phosphine hydrochloride], 0.2 mM phosphoenolpyruvate, crystallization by 0.9 M ammonium sulfate, 100 mM Tris, pH 7.9 to 8.0, and 1 to 5% PEG 400 |
| 2.5.1.54 | in complex with inhibitor 3-deoxy-D-arabinoheptulosonate-7-phosphate oxime |
| 2.5.1.54 | modeling of the three dimensional structure of the type II enzyme present in Arabidopsis thaliana and comparison with type I DAHPS. The enzyme belongs to the (beta/alpha)8 TIM barrel family. At the N-terminus of the Arabidopsis thaliana enzyme, there are three non-core helices, alpha0a (Ala72-Lys83), alpha0b (Ala94-Ala106) and alpha0c (Ala113-Val128), but no beta0, in contrast to the microbial type II DAHPS. Also, the (I/L)GAR motif in the type I DAHPS is substituted with xGxR in the case of type II DAHPS. A motif NK(/I)PGR(/K) is present in the sequences of type II DAHPS including At-DAHPS |
| 2.5.1.54 | molecular modeling of structure. The monomeric structure of Aro1A is a (beta/alpha)8 barrel structure. Phosphoenolpyruvate combines with residues R60, Q116, S119, K141, and R171 through eight hydrogen bonds. D-erythrose 4-phosphate combines with residues R60, K65, Q116, S119, K141, and R171 through nine hydrogen bonds |
| 2.5.1.54 | native and selenomethionine-substituted protein, in complex with phosphoenolpyruvate and Mn2+, mutant E24Q in complex with phosphoenolpyruvate and Mn2+ |
