Literature summary extracted from
Boughton, B.; Dobson, R.; Hutton, C.
The crystal structure of dihydrodipicolinate synthase from Escherichia coli with bound pyruvate and succinic acid semialdehyde: unambiguous resolution of the stereochemistry of the condensation product (2012), Proteins, 80, 2117-2122.
Application
EC Number |
Application |
Comment |
Organism |
---|
4.3.3.7 |
drug development |
the enzyme is an attractive target for the design and synthesis of herbicides and antibiotics |
Escherichia coli |
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.3.3.7 |
recombinant enzyme expression in Escherichia coli strain XL-1 Blue using plasmid pJG001 |
Escherichia coli |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.3.3.7 |
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/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
4.3.3.7 |
(S)-aspartate-4-semialdehyde + pyruvate |
Escherichia coli |
- |
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.3.3.7 |
Escherichia coli |
P0A6L2 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.3.3.7 |
recombinant enzyme 5.7fold from Escherichia coli strain XL-1 Blue |
Escherichia coli |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
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 |
Escherichia coli |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.3.3.7 |
(S)-aspartate-4-semialdehyde + pyruvate |
- |
Escherichia coli |
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
4.3.3.7 |
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
EC Number |
Synonyms |
Comment |
Organism |
---|
4.3.3.7 |
DHDPS |
- |
Escherichia coli |
4.3.3.7 |
dihydrodipicolinate synthase |
- |
Escherichia coli |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
4.3.3.7 |
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 |
4.3.3.7 |
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 |