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Literature summary extracted from
- Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase (2008), FEBS Lett., 582, 2923-2930.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 4.3.3.7 | pharmacology | enzyme structure analysis for design of novel therapeutics against bacterial pathogen | Staphylococcus aureus |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.3.3.7 | expressed in Escherichia coli BL21(DE3), full length dapA gene (DHDPS-FL) and C-terminal variant (DHDPS D228-295) lacking the three helical domains, pET22b vector | Staphylococcus aureus |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.3.3.7 | hanging-drop and sitting-drop method, solved in the native form and in complex with pyruvate at 2.3 A and 2.2 A resolution, respectively, single crystal grown in 2 M ammonium sulfate and 0.1 M Bis-Tris pH 6.5 used for data collection, processing and refinement statistics | Staphylococcus aureus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.3.7 | L-lysine | poor feedback inhibition by | Staphylococcus aureus |  |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.3.3.7 | 0.12 | - |
pyruvate | - |
Staphylococcus aureus | |
| 4.3.3.7 | 0.33 | - |
(S)-aspartate 4-semialdehyde | - |
Staphylococcus aureus | |
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 | Staphylococcus aureus | - |
dihydrodipicolinate + H2O | - |
? | |
| 4.3.3.7 | (S)-aspartate 4-semialdehyde + pyruvate | Staphylococcus aureus COL | - |
dihydrodipicolinate + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.3.3.7 | Staphylococcus aureus | Q5HG25 | - |
- |
| 4.3.3.7 | Staphylococcus aureus COL | Q5HG25 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.3.3.7 | gel filtration | Staphylococcus aureus |
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 | - |
quaternary structure different from other characterized homologues, dimer both in solution and in the crystal, catalytically important Lys-163 and the proton relay catalytic triad comprising Thr-46, Tyr-109 and Tyr-135 corresponds well with the enzyme homologue of Escherichia coli, deletion mutant lacking the three helical domains reveals a significant reduction in enzymatic activity, changes in the catalytic site upon pyruvate binding provide a structural basis for the ping-pong reaction mechanism, no feedback inhibition by lysine, free and substrate bound forms provide a structural rationale for catalytic mechanism, unique conformational features crucial for the design of specific non-competitive inhibitors | Staphylococcus aureus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.3.3.7 | (S)-aspartate 4-semialdehyde + pyruvate | - |
Staphylococcus aureus | dihydrodipicolinate + H2O | - |
? | |
| 4.3.3.7 | (S)-aspartate 4-semialdehyde + pyruvate | biosynthesis of (S)-lysine and meso-diaminopimelate, compounds of bacterial cell walls | Staphylococcus aureus | dihydrodipicolinate + H2O | - |
? | |
| 4.3.3.7 | (S)-aspartate 4-semialdehyde + pyruvate | - |
Staphylococcus aureus COL | dihydrodipicolinate + H2O | - |
? | |
| 4.3.3.7 | (S)-aspartate 4-semialdehyde + pyruvate | biosynthesis of (S)-lysine and meso-diaminopimelate, compounds of bacterial cell walls | Staphylococcus aureus COL | dihydrodipicolinate + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.3.3.7 | homodimer | in solution and in the crystal, gel filtration, crystallization and dynamic light scattering experiments | Staphylococcus aureus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.3.3.7 | DHDPS | - |
Staphylococcus aureus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.3.3.7 | 8 | - |
assay at | Staphylococcus aureus |
IC50 Value
| EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|---|
| 4.3.3.7 | 225 | - |
in presence of excess of substrates | Staphylococcus aureus | L-lysine | |
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