EC Number   |
Reaction |
Reference |
|---|
    4.3.3.7 | pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O |
- |
- |
| 4.3.3.7 | pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O |
ping-pong kinetic and catalytic mechanism involves a catalytic triad which consists of Tyr133, Thr44, and Tyr107, overview |
652939 |
| 4.3.3.7 | pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O |
ping-pong kinetic reaction mechanism |
729237 |
| 4.3.3.7 | pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O |
ping-pong mechanism, in which pyruvate binds as a Schiff base to an active-site lysine residue (Lys162 in Agrobacterium tumefaciens) |
-, 728891 |
| 4.3.3.7 | pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O |
ping-pong mechanism, pyruvate binds as a Schiff base to Lys161. After aldol reaction with L-aspartate-4-semialdehyde and transamination the product is released |
33922 |
| 4.3.3.7 | pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O |
pyruvate binds to the enzyme first by forming a Schiff base with the epsilon-amino group of Lys161. After release of the first water molecule L-aspartate-4-semialdehyde binds to the active site and the condensation reaction to form 2,3-dihydrodipicolinate takes place |
33912 |
| 4.3.3.7 | pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O |
reaction mechanism including Schiff base formation, tautomerization, and cyclization, overview |
713969 |
| 4.3.3.7 | pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O |
reaction steps, overview |
729694 |
| 4.3.3.7 | pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O |
the enzyme-catalyzed reaction is initiated by condensation of pyruvate with an active site lysine residue (Lys161 in Escherichia coli DHDPS) forming a Schiff base, ping-pong kinetic reaction mechanism via enamine intermediate, overview |
730908 |
| 4.3.3.7 | pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O |
the reaction is initiated by an nucleophilic attack of the epsilon-amino group of active site lysine to the C2 atom of pyruvate with subsequent imine formation. Tautomerization of the imine to the enamine creates the nucleophile necessary for the attack of the aldehyde group of L-aspartate semialdehyde. Cyclization of the substrate coupled with transamination leads to stepwise detachment from the active site |
33921 |
