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Literature summary for 4.3.3.7 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)

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

Crystallization (Commentary)

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

Inhibitors

Inhibitors Comment Organism Structure
(S)-lysine allosteric inhibitor Escherichia coli
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-aspartate 4-semialdehyde + pyruvate Escherichia coli
-
dihydrodipicolinate + H2O
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6L2
-
-

Purification (Commentary)

Purification (Comment) Organism
gel filtration Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-aspartate 4-semialdehyde + pyruvate
-
Escherichia coli dihydrodipicolinate + H2O
-
?
(S)-aspartate 4-semialdehyde + pyruvate reaction mechanism and active site analyzed, inhibition by the substrate analog beta-hydroxypyruvate Escherichia coli dihydrodipicolinate + H2O
-
?

Synonyms

Synonyms Comment Organism
DHDPS
-
Escherichia coli

Temperature Optimum [°C]

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

pH Optimum

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

Ki Value [mM]

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