Application | Comment | Organism |
---|---|---|
drug development | the enzyme is an attractive target for the design and synthesis of herbicides and antibiotics | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
recombinant enzyme expression in Escherichia coli strain XL-1 Blue using plasmid pJG001 | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
purified enzyme in complex with pyruvate and substrate analogue succinic acid semialdehyde, hanging drop vapor diffusion method, mixing of 0.003 ml of 8 mg/mL protein in 20 mM Tris-HCl, pH 8.0, with 0.0012 ml of precipitant solution containing 1.8 M K2HPO4, pH 10, and 0.0006 ml of N-octyl-beta-R-glucopyranoside 6% w/v, 4°C, 3-4 days, soaking in cryoprotectant solution containing 1.8 M K2HPO4, pH 10, glycerol 20% v/v, and 120 mM succinic acid semialdehyde and 40 mM pyruvate, X-ray diffraction structure determination and analysis at 2.3 A resolution | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-aspartate-4-semialdehyde + pyruvate | Escherichia coli | - |
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A6L2 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme 5.7fold from Escherichia coli strain XL-1 Blue | Escherichia coli |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-aspartate-4-semialdehyde + pyruvate | - |
Escherichia coli | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | the enzyme shows the typical homotetrameric form exhibited by bacterial DHDPS enzymes, present as a dimer of tight dimers. Each monomer consists of an N-terminal domain (residues 1-224) showing a parallel (beta/alpha)8-barrel (TIM barrel) motif. The smaller C-terminal domain, residues 224-292, is comprised of three alpha-helices | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
DHDPS | - |
Escherichia coli |
dihydrodipicolinate synthase | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme catalyses the first committed step in the lysine biosynthesis pathway, the condensation of pyruvate and (S)-aspartate semialdehyde to form (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid | Escherichia coli |
additional information | the catalytic site of DHDPS is situated at the C-terminal end of the TIM barrel where the pyruvate-binding residue, Lys161, lies in a solvent-accessible cleft with Arg138 capping the binding site. One-half of the active site is blocked by binding interactions of another monomer | Escherichia coli |