EC Number   |
|---|
    4.1.99.2 | - |
| 4.1.99.2 | analysis of crystal structure with bound competitive inhibitor 4-hydroxyphenylpropionate, PDB ID 1AX4 |
| 4.1.99.2 | hanging drop vapour diffusion method with 50 mM potassium phosphate (pH 8.0), 2 mM DTT, 0.2 M KCl, and 32.5% (w/v) PEG2000 for the apo-enzyme, and 50 mM triethanolamine buffer (pH 8.0), containing 0.5 mM PLP, 2 mM DTT, 0.4-0.8 M KCl, and 35-38% (w/v) PEG5000 for the holo-enzyme |
| 4.1.99.2 | in complex with L-methionine and L-phenylalanine, wild type and mutant Y71F |
| 4.1.99.2 | purified wild-type enzyme in ternary complex with pyridine N-oxide and the L-Ala quinonoid reaction intermediate by soaking wild-type TPL crystals in the stabilization solution containing 40% w/v PEG 5000 MME, 50 mM triethanolamine, pH 8.0, 0.25 M KCl, 0.2 mM pyridoxal 5'-phosphate, 0.5 mM dithiothreitol, with 100 mM L-Ala and a saturating concentration of pyridine N-oxide for 20 s, and purified Y71F or F448H mutant enzymes with bound substrate in quinoid intermediate state by soaking the crystals in the same stabilizing solution but with addition of 10 mM 3-fluoro-L-Tyr for 30 s, X-ray diffraction structure determination and analysis at 2.05-2.25 A resolution |
| 4.1.99.2 | the quinonoid intermediates of tyrosine phenol-lyase with L-alanine and L-methionine are trapped in the crystalline state and their structures are determined at 1.9 A and 1.95 A resolution, respectively |
| 4.1.99.2 | tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid |
