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Literature summary for 4.3.3.7 extracted from

  • Muscroft-Taylor, A.C.; Catchpole, R.J.; Dobson, R.C.; Pearce, F.G.; Perugini, M.A.; Gerrard, J.A.
    Disruption of quaternary structure in Escherichia coli dihydrodipicolinate synthase (DHDPS) generates a functional monomer that is no longer inhibited by lysine (2010), Arch. Biochem. Biophys., 503, 202-206.
    View publication on PubMed
Search for more literature for 4.3.3.7

Cloned(Commentary)

Cloned (Comment) Organism
gene dapA, overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 Star (DE3) Escherichia coli

Protein Variants

Protein Variants Comment Organism
L197D/Y107W site-directed mutagenesis, the mutant forms a monomer that is catalytically active, but with reduced catalytic efficiency, displaying 8% of the specific activity of the wild-type enzyme. The Michaelis constants for the substrates pyruvate and for (S)-aspartate semialdehyde increase by an order of magnitude. L197D/Y107W is expressed as a folded monomer Escherichia coli
additional information disruption of quaternary structure of DHDPS generates a functional monomer that is no longer inhibited by lysine, overview Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
L-lysine inhibition of the tetrameric wild-type enzyme, but not of the disrupted minimeric mutant enzyme. Allosteric binding by two molecules of (S)-lysine at the DHDPS tight-dimer interface cleft has been observed to operate via a cooperative mechanism and to result in incomplete partial mixed inhibition, inhibition kinetics, overview Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic study: the wild-type enzyme shows a ping pong mechanism, while the monomeric mutant L197D/Y107W shows ternary-complex mechanism Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate 4-semialdehyde + pyruvate Escherichia coli
-
 (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 gene dapA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography and gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate 4-semialdehyde + pyruvate
-
 Escherichia coli (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O
-
 ?
additional information the quaternary structure plays a significant role in substrate specificity, overview Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More disruption of quaternary structure of DHDPS generates a functional monomer that is no longer inhibited by lysine, overview Escherichia coli
tetramer
-
 Escherichia coli

Synonyms

Synonyms Comment Organism
DHDPS
-
 Escherichia coli

Temperature Optimum [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
20 95 purified recombinnat wild-type enzyme Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
9.8
-
 pyruvate pH 8.0, 30°C, recombinant wild-type enzyme Escherichia coli
9.8
-
 L-aspartate 4-semialdehyde pH 8.0, 30°C, recombinant wild-type enzyme Escherichia coli

pH Optimum

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

General Information

General Information Comment Organism
additional information monomeric species exhibit an enhanced propensity for aggregation and inactivation, indicating that whilst the oligomerization is not an intrinsic criterion for catalysis, higher oligomeric forms may benefit from both increased catalytic efficiency and diminished aggregation propensity Escherichia coli
physiological function DHDPS catalyses a branch point reaction the condensation of pyruvate and (S)-aspartate beta-semialdehyde to form an unstable product, (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid, which is ultimately advanced to the final metabolites (S)-lysine and meso-diaminopimelate Escherichia coli