EC Number |
Reaction |
Reference |
---|
4.3.1.17 | 2-aminoprop-2-enoate = 2-iminopropanoate |
(1b), spontaneous |
- |
4.3.1.17 | 2-iminopropanoate + H2O = pyruvate + NH3 |
(1c), spontaneous |
- |
4.3.1.17 | L-serine = 2-aminoprop-2-enoate + H2O |
(1a) |
- |
4.3.1.17 | L-serine = pyruvate + NH3 |
(overall reaction) |
- |
4.3.1.17 | L-serine = pyruvate + NH3 |
catalytic mechanism |
691069 |
4.3.1.17 | L-serine = pyruvate + NH3 |
pre-steady-state kinetic analysis of L-serine binding to lpLSD demonstrates that L-serine binds to a second noncatalytic site and produces a conformational change in the enzyme. The rate of this conformational change is too slow for its participation in the catalytic cycle but rather occurs prior to catalysis to produce an activated form of the enzyme |
729219 |
4.3.1.17 | L-serine = pyruvate + NH3 |
reaction analysis by ab initio quantum mechanical/molecular mechanical method, the reaction involves a Schiff base formation step and a proton-relaying mechanism involving the phosphate of the cofactor in the beta-hydroxyl-leaving step following sequentially after the elimination of the alpha-proton, leading to a single but sequential alpha,beta-elimination step. The rate-limiting transition state is specifically stabilized by the enzyme environment, catalytic mechanism involving Lys41 in the active site, detailed overview |
693834 |