Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Otero, L.H.; Beassoni, P.R.; Boetsch, C.; Lisa, A.T.; Domenech, C.E.
    Different effects of Mg2+ and Zn2+ on the two sites for alkylammonium compounds in Pseudomonas aeruginosa phosphorylcholine phosphatase (2011), Enzyme Res., 2011, 918283.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.75 gene pchP, expression of His-tagged enzyme in Escherichia coli strain BL21 Pseudomonas aeruginosa

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.75 Chlorocholine
-
 Pseudomonas aeruginosa
3.1.3.75 choline
-
 Pseudomonas aeruginosa
3.1.3.75 decamethonium
-
 Pseudomonas aeruginosa
3.1.3.75 hexamethonium
-
 Pseudomonas aeruginosa
3.1.3.75 additional information inhibition mechanism of alkylammonium compounds, enzyme PchP contains two sites for alkylammonium compounds: one in the catalytic site near the metal ion-phosphoester pocket, and the other in an inhibitory site responsible for the binding of the alkylammonium moiety Pseudomonas aeruginosa
3.1.3.75 phosphocholine substrate inhibition at high concentration Pseudomonas aeruginosa
3.1.3.75 Tetramethylammonium chloride
-
 Pseudomonas aeruginosa
3.1.3.75 trimethylamine
-
 Pseudomonas aeruginosa
3.1.3.75 Zn2+ Zn2+ is an activator at pH 5.0 but an reversible inhibitor at pH 7.4. Activation or inhibition of PchP by Zn2+ is caused by the transition from octahedral to tetrahedral geometry in the coordination sphere of the metal ion Pseudomonas aeruginosa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.75 Cu2+ activates Pseudomonas aeruginosa
3.1.3.75 Mg2+ Mg2+ is an equal activator for the enzyme at pH 5.0 and at pH 7.4. Mg2+ produces a relaxed or open conformation Pseudomonas aeruginosa
3.1.3.75 additional information Zn2+ has 1000fold stronger affinity for PchP compared to Mg2+ Pseudomonas aeruginosa
3.1.3.75 Zn2+ Zn2+ is an activator at pH 5.0 but an reversible inhibitor at pH 7.4. Activation or inhibition of PchP by Zn2+ is caused by the transition from octahedral to tetrahedral geometry in the coordination sphere of the metal ion 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 gene pchP
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.75 additional information phosphorylcholine phosphatase catalyzes the hydrolysis of 4-nitrophenylphosphate Pseudomonas aeruginosa ?
-
 ?
3.1.3.75 phosphocholine + H2O
-
 Pseudomonas aeruginosa choline + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.75 More the enzyme belongs to the haloacid dehalogenase superfamily Pseudomonas aeruginosa
3.1.3.75 PChP
-
 Pseudomonas aeruginosa
3.1.3.75 phosphorylcholine phosphatase
-
 Pseudomonas aeruginosa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.75 37
-
 assay at Pseudomonas aeruginosa

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.3.75 additional information
-
 additional information inhibition kinetics for alkylammonium compounds trimethylamine, tetramethylammonium chloride, choline, chlorocholine, hexamethonium, and decamethonium, in presence of Zn2+ or Mg2+, overview Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
3.1.3.75 additional information catalytic mechanism of phosphocholine with Pcho as the substrate, Mg2+ or Zn2+ as activators, and alkylammonium compounds as inhibitors, overview. Zn2+ induces a conformational change in the active center that is communicated to the inhibitory site, producing a compact or closed structure. In contrast, Mg2+ produces a relaxed or open conformation Pseudomonas aeruginosa