EC Number   |
Reference |
|---|
    2.3.1.133 | in complex with CoA and 4-coumaroyl-shikimate. The 4-coumaroyl-shikimate contacts the enzyme via the phenolic group and carbonyl group of the 4-coumaroyl portion. The shikimate portion contacts the enzyme through both the carboxyl and hydroxyl groups. In the protocatechuate ternary complex, protocatechuate binds in a very similar manner to shikimate, with the carboxyl group making a tight salt bridge with Arg369, and the C3 hydroxyl group interacting with the nitrogen NE2 of His163 |
736977 |
| 2.3.1.133 | purified recombinant HCT, sitting drop technique, mixing of 100 nl of 20 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, 5 mM 2-mercaptoethanol, with 100 nl of precipitant solution containing 1.6 M magnesium sulfate, 0.1 M MES pH 6.5, 20°C, 2 months, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement |
718519 |
| 2.3.1.133 | structures in its apo-form and ternary complex with shikimate and 4-coumaroyl-CoA, which is converted to its product during crystal soaking. Residues threonine36, serine38, tyrosine40, histidine162, arginine371, and threonine384 are involved in catalysis and specificity. Histidine162 and threonine36 play a role in the catalytic mechanism. Substrate binding should occur sequentially, with 4-coumaroyl-CoA binding prior to the acyl acceptor molecule. Comparison of the structure of sorghum HCT with the HCT involved in chlorogenic acid synthesis in Coffea canephora |
737024 |
