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Literature summary extracted from
- 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.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.3.3.7 | gene dapA, overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 Star (DE3) | Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.3.3.7 | 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 |
| 4.3.3.7 | additional information | disruption of quaternary structure of DHDPS generates a functional monomer that is no longer inhibited by lysine, overview | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.3.7 | 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]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.3.3.7 | 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)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.3.3.7 | L-aspartate 4-semialdehyde + pyruvate | Escherichia coli | - |
(S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.3.3.7 | Escherichia coli | - |
gene dapA | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.3.3.7 | 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)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.3.3.7 | L-aspartate 4-semialdehyde + pyruvate | - |
Escherichia coli | (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O | - |
? | |
| 4.3.3.7 | additional information | the quaternary structure plays a significant role in substrate specificity, overview | Escherichia coli | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.3.3.7 | More | disruption of quaternary structure of DHDPS generates a functional monomer that is no longer inhibited by lysine, overview | Escherichia coli |
| 4.3.3.7 | tetramer | - |
Escherichia coli |
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 |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.3.3.7 | 20 | 95 | purified recombinnat wild-type enzyme | Escherichia coli |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.3.3.7 | 9.8 | - |
pyruvate | pH 8.0, 30°C, recombinant wild-type enzyme | Escherichia coli | |
| 4.3.3.7 | 9.8 | - |
L-aspartate 4-semialdehyde | pH 8.0, 30°C, recombinant wild-type enzyme | Escherichia coli | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.3.3.7 | 8 | - |
assay at | Escherichia coli |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.3.3.7 | 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 |
| 4.3.3.7 | 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 |
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