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Literature summary extracted from

  • Dobson, R.C.; Griffin, M.D.; Devenish, S.R.; Pearce, F.G.; Hutton, C.A.; Gerrard, J.A.; Jameson, G.B.; Perugini, M.A.
    Conserved main-chain peptide distortions: a proposed role for Ile203 in catalysis by dihydrodipicolinate synthase (2008), Protein Sci., 17, 2080-2090.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.3.7 expressed in Escherichia coli XL1-blue, pBluescript vector, recombinant protein Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.3.7 in complex with beta-hydroxypyruvate, hanging drop vapor-diffusion method, data processing and refinement statistics Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.3.7 (S)-lysine allosteric inhibitor Escherichia coli
4.3.3.7 3-hydroxy-2-oxopropanoate time-dependent inhibition, qualitatively followed by mass spectrometry, initial noncovalent adduct formation, followed by the slow formation of the covalent adduct 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
-
 dihydrodipicolinate + 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 gel filtration Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3.3.7 additional information
-
 role of beta-hydroxypruvate in regulating biosynthesis of dihydrodipicolinate unknown, crystal structure of DHDPS enzyme complexed with beta-hydroxypyruvate solved, active site shows the presence of the inhibitor covalently bound to Lys161, hydroxyl group of inhibitor is hydrogen-bonded to main-chain carbonyl of Ile203, evidence for a catalytic function played by this peptide unit, highly strained torsion angle conserved in active site of other homologous enzyme, points to critical role in catalysis 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 dihydrodipicolinate + H2O
-
 ?
4.3.3.7 (S)-aspartate 4-semialdehyde + pyruvate reaction mechanism and active site analyzed, inhibition by the substrate analog beta-hydroxypyruvate Escherichia coli dihydrodipicolinate + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.3.3.7 DHDPS
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.3.3.7 30
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.3.7 8
-
 assay at Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.3.3.7 0.21
-
 3-hydroxy-2-oxopropanoate time-dependent inhibition, value similar to that of (S)-lysine Escherichia coli