EC Number   |
Reaction |
Reference |
|---|
    4.1.1.48 | 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O |
in some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [2.4.2.18 (anthranilate phosphoribosyltransferase), 4.1.3.27 (anthranilate synthase), 4.2.1.20 (tryptophan synthase) and 5.3.1.24 (phosphoribosylanthranilate isomerase)] |
- |
| 4.1.1.48 | 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O |
mechanism, structures of two putative catalytic intermediates |
652887 |
| 4.1.1.48 | 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O |
molecular dynamics simulation study of the enzyme-substrate complex at room temperature and at 110°C. Relative specific activity increases 4200fold up to 110°C. Active site residues K53 and K110 control the binding of substrate in the favorable orientation for the general acid-catalyzed intramolecular ring formation reaction |
665298 |
| 4.1.1.48 | 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O |
molecular dynamics study at different temperatures. K110 is the general acid, E210 the general base. At higher temperature, the enzyme-substrate electrostatic interaction favors the binding of the substrate in near attack conformation, at lower temperature, the substrate is bound in nonreactive conformation |
666710 |
