4-hydroxy-tetrahydrodipicolinate synthase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O. [PMID:8993314, RHEA:34171]

4-Hydroxy-tetrahydrodipicolinate synthase (HTPS) activity is a critical step in the biosynthesis of diaminopimelate (DAP), a key precursor for the synthesis of lysine and peptidoglycan, a major structural component of bacterial cell walls. HTPS catalyzes the condensation of L-aspartate semialdehyde and pyruvate to form 4-hydroxy-tetrahydrodipicolinate (HTPA), a central intermediate in the DAP biosynthesis pathway. The enzyme utilizes a highly conserved active site containing a pyridoxal phosphate (PLP) cofactor. The reaction mechanism involves the following key steps: 1) PLP forms a Schiff base with the amino group of L-aspartate semialdehyde. 2) The Schiff base is then deprotonated by a base, leading to the formation of a quinonoid intermediate. 3) The quinonoid intermediate undergoes nucleophilic attack by pyruvate, resulting in the formation of HTPA. 4) HTPA is released from the active site, and the enzyme returns to its initial state. The activity of HTPS is essential for bacterial growth and survival, making it a potential target for the development of novel antimicrobial agents.'
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Proteins (1)

Compounds (4)