EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.5.1.55 | purified recombinant mutant enzymes, hanging-drop vapor diffusion, mixing of 0.002 ml of protein solution containing 20 mg/ml protein in 10 mM BTP, pH 7.5, with 0.002 ml of reservoir solution containing 100 mM sodium acetate, pH 4.6, and 0.6-3.0 M NaCl, equilibration against 0.5 ml reservoir solution, 20°C, 24 h, X-ray diffraction structure determination and analysis at 1.75-2.10 A resolution | Neisseria meningitidis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.5.1.55 | F114A | site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis | Neisseria meningitidis |
2.5.1.55 | F114R | site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type, structure analysis | Neisseria meningitidis |
2.5.1.55 | F114R/R117A | site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type, structure analysis | Neisseria meningitidis |
2.5.1.55 | F114R/R117Q | site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis | Neisseria meningitidis |
2.5.1.55 | F114R/R117Q/F139G | site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis | Neisseria meningitidis |
2.5.1.55 | F139G | site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis | Neisseria meningitidis |
2.5.1.55 | R117K | site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis | Neisseria meningitidis |
2.5.1.55 | R117Q | site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis | Neisseria meningitidis |
EC Number | General Stability | Organism |
---|---|---|
2.5.1.55 | Cd2+ destabilizes the enzyme, overview | Neisseria meningitidis |
2.5.1.55 | substrate phosphoenolpyruvate stabilizes the wild-type and mutant enzymes | Neisseria meningitidis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.5.1.55 | additional information | - |
additional information | Michaelis-Menten kinetics | Neisseria meningitidis | |
2.5.1.55 | 0.0025 | - |
phosphoenolpyruvate | pH and temperature not specified in the publication | Neisseria meningitidis | |
2.5.1.55 | 0.012 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication | Neisseria meningitidis | |
2.5.1.55 | 0.014 | - |
phosphoenolpyruvate | pH and temperature not specified in the publication, mutant F139A | Neisseria meningitidis | |
2.5.1.55 | 0.022 | - |
phosphoenolpyruvate | pH and temperature not specified in the publication, R117K | Neisseria meningitidis | |
2.5.1.55 | 0.058 | - |
phosphoenolpyruvate | pH and temperature not specified in the publication, mutant F114A | Neisseria meningitidis | |
2.5.1.55 | 0.095 | - |
phosphoenolpyruvate | pH and temperature not specified in the publication, mutant F114R | Neisseria meningitidis | |
2.5.1.55 | 0.285 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, mutant F114R | Neisseria meningitidis | |
2.5.1.55 | 0.594 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, mutant F139A | Neisseria meningitidis | |
2.5.1.55 | 0.816 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, R117K | Neisseria meningitidis | |
2.5.1.55 | 0.873 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, mutant F114A | Neisseria meningitidis | |
2.5.1.55 | 2.742 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, mutant F114R/R117Q | Neisseria meningitidis | |
2.5.1.55 | 3.21 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, R117Q | Neisseria meningitidis | |
2.5.1.55 | 3.6 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, F114R/R117Q/F139G | Neisseria meningitidis | |
2.5.1.55 | 3.7 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, mutant F114R/R117A | Neisseria meningitidis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.5.1.55 | Cd2+ | destabilizes the enzyme, overview | Neisseria meningitidis | |
2.5.1.55 | additional information | metal-independent enzyme. Mn2+ or Co2+ have no effect on enzyme stability | Neisseria meningitidis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.55 | phosphoenolpyruvate + D-arabinose 5-phosphate + H2O | Neisseria meningitidis | - |
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.55 | Neisseria meningitidis | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.55 | phosphoenolpyruvate + D-arabinose 5-phosphate + H2O | - |
Neisseria meningitidis | 3-deoxy-D-manno-octulosonate 8-phosphate + phosphate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.5.1.55 | tetramer | the enzyme adopts a homotetrameric associations with its active site close to one of the interfaces. The conserved PAFLxR motif in KDO8PS on the short beta4alpha4 loop of the (beta/alpha)8 barrel, form part of this interface and provide key contacts with substrates | Neisseria meningitidis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.5.1.55 | 3-deoxy-D-manno-octulosonate 8-phosphate synthase | - |
Neisseria meningitidis |
2.5.1.55 | KDO8PS | - |
Neisseria meningitidis |
2.5.1.55 | NmeKDO8PS | - |
Neisseria meningitidis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.5.1.55 | 0.01 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, R117A | Neisseria meningitidis | |
2.5.1.55 | 0.108 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, mutant F114R/R117A | Neisseria meningitidis | |
2.5.1.55 | 0.14 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, F114R/R117Q/F139G | Neisseria meningitidis | |
2.5.1.55 | 0.27 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, mutant F114R/R117Q | Neisseria meningitidis | |
2.5.1.55 | 1.06 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, R117Q | Neisseria meningitidis | |
2.5.1.55 | 3 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, mutant F114R | Neisseria meningitidis | |
2.5.1.55 | 4.8 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, R117K | Neisseria meningitidis | |
2.5.1.55 | 6.1 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, mutant F114A | Neisseria meningitidis | |
2.5.1.55 | 8 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, wild/type enzyme | Neisseria meningitidis | |
2.5.1.55 | 8.6 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, mutant F139A | Neisseria meningitidis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.5.1.55 | evolution | KDO8PS is evolutionarily and structurally related to the first enzyme of the shikimate pathway, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAH7PS, EC 2.5.1.54), which uses erythrose 4-phosphate in place of arabinose 5-phosphate. Both KDO8PS and type Ibeta DAH7PS enzymes adopt similar homotetrameric associations with their active sites close to one of the interfaces | Neisseria meningitidis |
2.5.1.55 | physiological function | the enzyme catalyzes the reaction between phosphoenolpyruvate and arabinose 5-phosphate in the first committed step in the pathway to 3-deoxy-D-manno-octulosonate, a component in the cell wall of Gram-negative bacteria | Neisseria meningitidis |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.5.1.55 | 0.029 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, mutant F114R | Neisseria meningitidis | |
2.5.1.55 | 0.039 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, mutant F114R/R117Q | Neisseria meningitidis | |
2.5.1.55 | 0.1 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, mutant F114R/R117A | Neisseria meningitidis | |
2.5.1.55 | 0.33 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, R117Q | Neisseria meningitidis | |
2.5.1.55 | 5.9 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, F114R/R117Q/F139G | Neisseria meningitidis | |
2.5.1.55 | 7 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, mutant F139A | Neisseria meningitidis | |
2.5.1.55 | 11 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication, mutant F114A | Neisseria meningitidis | |
2.5.1.55 | 14 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication | Neisseria meningitidis | |
2.5.1.55 | 660 | - |
D-arabinose 5-phosphate | pH and temperature not specified in the publication | Neisseria meningitidis |