Literature summary extracted from
Otero, L.H.; Beassoni, P.R.; Domenech, C.E.; Lisa, A.T.; Albert, A.
Crystallization and preliminary X-ray diffraction analysis of Pseudomonas aeruginosa phosphorylcholine phosphatase (2010), Acta Crystallogr. Sect. F, 66, 957-960.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.1.3.75 |
gene pchP327, recombinant expression with a N-terminal fusion to an MGSSHHHHHHSSGLVPRGSH tag in Escherichia coli BL21, expression of N-terminal His6-tagged PchP in Escherichia coli |
Pseudomonas aeruginosa |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.1.3.75 |
purified recombinant enzyme, sitting drop vapour diffusion method, 250 nl of 10 mg/ml protein in 200 mM NaCl, 10 mM Tris-HCl, pH 8.0, are mixed with 250 nl well solution and are equilibrated against 0.5 ml well solution containing 0.1 M Bis-Tris, pH 5.5, 0.2 M MgCl2, 25% PEG 3350, producing clustered plate-like microcrystals, or by microbatch method mixing 0.001 ml of protein solution containing 10 mg/ml in 200 mM NaCl, 20 mM Bis-Tris, pH 5.5, with 0.002 ml precipitant solution, cryoprotection by a quick soak in 0.1 M Bis-Tris pH 5.5, 0.2 M MgCl2, 25% PEG 3350, 15% glycerol, X-ray diffraction structure determination and analysis at 2.7 A resolution |
Pseudomonas aeruginosa |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.1.3.75 |
Zn2+ |
inhibition produced by Zn2+ at pH 7.4 represents a change from octahedral to tetrahedral coordination geometry which is produced by hydrolysis of the Zn-hexacoordinated complex |
Pseudomonas aeruginosa |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.1.3.75 |
Cu2+ |
dependent on divalent cations Mg2+, Zn2+ or Cu2+ |
Pseudomonas aeruginosa |
|
3.1.3.75 |
Mg2+ |
dependent on divalent cations Mg2+, Zn2+ or Cu2+ |
Pseudomonas aeruginosa |
|
3.1.3.75 |
Zn2+ |
dependent on divalent cations Mg2+, Zn2+ or Cu2+ |
Pseudomonas aeruginosa |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
3.1.3.75 |
37000 |
- |
2 * 37000, about, recombinant His6-tagged enzyme, SDS-PAGE |
Pseudomonas aeruginosa |
3.1.3.75 |
60000 |
- |
about, recombinant His6-tagged enzyme, gel filtration |
Pseudomonas aeruginosa |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
3.1.3.75 |
phosphocholine + H2O |
Pseudomonas aeruginosa |
- |
choline + phosphate |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.1.3.75 |
Pseudomonas aeruginosa |
Q9HTR2 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.1.3.75 |
recombinant N-terminally His6-tagged PchP from Escherichia coli by nickel affinity chromatography |
Pseudomonas aeruginosa |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.1.3.75 |
phosphocholine + H2O |
- |
Pseudomonas aeruginosa |
choline + phosphate |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.1.3.75 |
dimer |
2 * 37000, about, recombinant His6-tagged enzyme, SDS-PAGE |
Pseudomonas aeruginosa |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.1.3.75 |
More |
PchP belongs to the HAD superfamily |
Pseudomonas aeruginosa |
3.1.3.75 |
PChP |
- |
Pseudomonas aeruginosa |
3.1.3.75 |
phosphorylcholine phosphatase |
- |
Pseudomonas aeruginosa |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
3.1.3.75 |
physiological function |
possible importance of PchP in the pathogenesis of Pseudomonas aeruginosa |
Pseudomonas aeruginosa |