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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.
    View publication on PubMed

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