Crystallization (Comment) | Organism |
---|---|
purified recombinant enzyme complexed with inhibitors (S)-phospholactate, (R)-phospholactate, and vinyl phosphonate, hanging drop vapour diffusion method, mixing of 0.001 ml of 10 mg/mL protein in 10 mM bis(tris(hydroxymethyl)methylamino)propane, pH 7.3, and 5 mM inhibitor, with 0.001 ml of crystallisation buffer containing 0.1 Tris HCl, pH 7.3, 0.2 M trimethyl-amino-N-oxide, 0.4 mM MnSO4, and 15-20% w/v PEG 2000MME, equilibration over 0.5 ml of reservoir solution, 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.76-2.34 A resolution | Neisseria meningitidis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(R)-phospholactate | - |
Neisseria meningitidis | |
(S)-phospholactate | - |
Neisseria meningitidis | |
additional information | binding structure determination and analysis, overview. The side chains of enzyme residues Lys188, Arg167 and Arg236 and the main chain peptide N of Ala166 that interact with the phosphate moiety of phosphoenolpyruvate form similar interactions with the phosphate or phosphonate functionalities of the three ligands, consistent with this portion of each inhibitor being able to mimic the phosphoenolpyruvate binding characteristics well. The tetrameric quaternary structures of enzyme NmeDAH7PS bound with (S)-phospholactate and vinyl phosphonate are identical to that of the isomorphous phosphoenolpyruvate-bound parent structure, PDB ID 4HSN. The increased inhibitor potency observed for the vinyl phosphonate over the (R)-phospholactate suggests that the active site is better prepared to accommodate a planar rather than tetrahedral intermediate | Neisseria meningitidis | |
vinyl phosphonate | - |
Neisseria meningitidis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Neisseria meningitidis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | required, Mn2+ coordinates the PEP carboxylate functionality and a water molecule | Neisseria meningitidis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O | Neisseria meningitidis | - |
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Neisseria meningitidis | Q9K169 | gene aroG | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate | proposed mechanism of catalysis of NmeDAH7PS showing key nucleophilic role for active site WAT1, overview | Neisseria meningitidis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O | - |
Neisseria meningitidis | 3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate | - |
? | |
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O | phosphoenolpyruvate binding structure analysis | Neisseria meningitidis | 3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase | - |
Neisseria meningitidis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Neisseria meningitidis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.8 | - |
assay at | Neisseria meningitidis |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0039 | - |
vinyl phosphonate | pH 6.8, 25°C, recombinant enzyme | Neisseria meningitidis | |
0.099 | - |
(R)-phospholactate | pH 6.8, 25°C, recombinant enzyme | Neisseria meningitidis | |
0.36 | - |
(S)-phospholactate | pH 6.8, 25°C, recombinant enzyme | Neisseria meningitidis |