EC Number   |
Natural Substrates |
|---|
    4.3.3.7 | (S)-aspartate 4-semialdehyde + pyruvate |
- |
| 4.3.3.7 | (S)-aspartate 4-semialdehyde + pyruvate |
branch point reaction in the biosynthesis of lysine |
| 4.3.3.7 | (S)-aspartate 4-semialdehyde + pyruvate |
first step in the biosynthesis of lysine, overview |
| 4.3.3.7 | (S)-aspartate 4-semialdehyde + pyruvate |
catalyses the branch point in lysine biosynthesis |
| 4.3.3.7 | (S)-aspartate-4-semialdehyde + pyruvate |
- |
| 4.3.3.7 | (S)-aspartate-4-semialdehyde + pyruvate |
the enzyme-catalyzed reaction is initiated by condensation of pyruvate with an active site Lys161 forming a Schiff base. Subsequent tautomerization to the enamine and aldol-type reaction with (S)-aspartate-4-semialdehyde then generates an acyclic enzyme-bound intermediate. Transimination of the acyclic intermediate yields the cyclic alcohol (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid, with simultaneous release of the active site lysine residue |
| 4.3.3.7 | L-aspartate 4-semialdehyde + pyruvate |
- |
| 4.3.3.7 | L-aspartate-4-semialdehyde + pyruvate |
- |
| 4.3.3.7 | L-aspartate-4-semialdehyde + pyruvate |
biosynthesis of lysine via the diaminopimelate pathway |
| 4.3.3.7 | L-aspartate-4-semialdehyde + pyruvate |
synthesis of the precursor of dipicolinic acid which plays a key role in bacterial sporulation process |
