EC Number   |
Reaction |
Reference |
|---|
    4.1.99.1 | L-tryptophan + H2O = indole + pyruvate + NH3 |
- |
- |
| 4.1.99.1 | L-tryptophan + H2O = indole + pyruvate + NH3 |
an active site base is essential for activity, and alpha-deuterated substrate exhibits modest primary isotope effects on kcat and kcat/Km, suggesting that substrate deprotonation is partially rate-limiting. Pre-steady state kinetics with enzyme TIL show rapid formation of an external aldimine intermediate, followed by deprotonation to give a quinonoid intermediate absorbing at about 500 nm. The mechanism of TIL requires both substrate strain and acid/base catalysis, and substrate strain is probably responsible for the very high substrate specificity of TIL. Acid-base catalysis mechanism of TIL, overview. The indole ring is preorganized into the active conformation before alpha-deprotonation occurs |
747245 |
| 4.1.99.1 | L-tryptophan + H2O = indole + pyruvate + NH3 |
an active site base is essential for activity, and alpha-deuterated substrate exhibits modest primary isotope effects on kcat and kcat/Km, suggesting that substrate deprotonation is partially rate-limiting. Pre-steady state kinetics with enzyme TIL show rapid formation of external an aldimine intermediate, followed by deprotonation to give a quinonoid intermediate absorbing at about 500 nm. The mechanism of TIL requires both substrate strain and acid/base catalysis, and substrate strain is probably responsible for the very high substrate specificity of TIL. Acid-base catalysis mechanism of TIL, overview. The indole ring is preorganized into the active conformation before alpha-deprotonation occurs |
747245 |
| 4.1.99.1 | L-tryptophan + H2O = indole + pyruvate + NH3 |
catalyses the reaction in which L-tryptophan is degraded to indole, pyruvate and ammonia via alpha,beta-elimination and beta-replacement mechanisms |
746651 |
| 4.1.99.1 | L-tryptophan + H2O = indole + pyruvate + NH3 |
in the reverse direction NH4+ interacts with bound pyridoxal 5'-phosphate to form an imine. Pyruvate is the second substrate, indole the third. alpha-Aminoacrylate functions as a common enzyme-bound intermediate in both synthetic and degradative reactions |
37357 |
| 4.1.99.1 | L-tryptophan + H2O = indole + pyruvate + NH3 |
mechanism |
650374, 650435, 652265 |
| 4.1.99.1 | L-tryptophan + H2O = indole + pyruvate + NH3 |
mechanism that requires two catalytic bases |
37334 |
| 4.1.99.1 | L-tryptophan + H2O = indole + pyruvate + NH3 |
mechanism, solvent effects |
651028 |
| 4.1.99.1 | L-tryptophan + H2O = indole + pyruvate + NH3 |
proposed mechanism of tryptophan indole-lyase, overview |
746909 |
| 4.1.99.1 | L-tryptophan + H2O = indole + pyruvate + NH3 |
quinonoid intermediate formation involving Tyr71 and Cys298, mechanism, active site preorganization, overview |
726995 |
