EC Number   |
|---|
    1.3.1.12 | in complex with NAD+, by hanging drop vapor diffusion technique at room temperature, one modified nucleotide-binding domain and a novel helical prephenate binding domain, active site formed at the domain interface and shared between the subunits of the dimer, access to active site may be regulated via a gated mechanism, modulated by an ionic network involving a conserved arginine, active site residues include Ser126 and Lys246 and the catalytic His147, two functional domains of chorismate mutase-prephenate dehydrogenase are interdependent |
| 1.3.1.12 | prephenate dehydrogenase bound with NAD+ plus either 4-hydroxyphenylpyuvate, 4-hydroxyphenylpropionate, or L-tyrosine. Resiudes His147 and Arg250 are key catalytic and binding groups, respectively, and Ser126 participates in both catalysis and substrate binding through the ligand 4-hydroxyl group. Inhibitor tyrosine binds directly to the active site of the enzyme and not to an allosteric site |
| 1.3.1.12 | prephenate dehydrogenase component of the TyrA protein from strain Rd KW20 in complex with inhibitor tyrosine and cofactor NAD+, sitting drop vapour diffusion method, 200 nl of 19.6 mg/ml protein in 20 mM HEPES pH 8.0, 200 mM NaCl, 40 mM imidazole, 1 mM TCEP are mixed with 200 nl reservoir solution containing 0.04 M potassium dihydrogen phosphate, 20.0% v/v glycerol and 16.0% w/v PEG 8000, X-ray diffrraction structure determination and analysis at 2.0 A resolution |
| 1.3.1.12 | structure of a ternary complex with NAD+ and tyrosine to 2.2 A resolution, a binary complex with tyrosine, and a structure of an isolated ACT domain dimer |
| 1.3.1.12 | to 2.1 A resolution. The N-terminal alpha/beta domain has a Rossman fold for binding a NAD+ molecule. The C-terminal domain adopts a helical architecture and is involved in homo-dimerization. NAD+ binding stabilizes the active site and facilitates the substrate, prephenate, binding |
