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Literature summary for 3.1.3.75 extracted from

  • Domenech, C.E.; Otero, L.H.; Beassoni, P.R.; Lisa, A.T.
    Phosphorylcholine phosphatase: A peculiar enzyme of Pseudomonas aeruginosa (2011), Enzyme Res., 2011, 561841.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.75

Cloned(Commentary)

Cloned (Comment) Organism
gene pchP, phylogenetic tree, regulation of pchP gene expression is under the control of GbdR and NtrC. PchP expression in Escherichia coli as an N-terminal fusion to intein or a histidine tag Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
additional information site-directed mutagenesis of the aspartyl, D31, D33, and threonyl, T35, residues of motif I, of the seryl, S166, residue of motif II, and of the lysyl, K242, glycyl, G261, and aspartyl residues, D262, D265, and D267, of motif III Pseudomonas aeruginosa

Inhibitors

Inhibitors Comment Organism Structure
Acetylcholine
-
 Pseudomonas aeruginosa
betaine
-
 Pseudomonas aeruginosa
choline
-
 Pseudomonas aeruginosa
additional information the enzyme contains two sites for alkylammonium compounds, one of which is located in the catalytic site near the metal ion-phosphoester pocket, while the other one is located in an inhibitory site responsible for the binding of the alkylammonium moiety. Both sites are close to each other and interact through the residues 42E, 43E and 82YYY84 Pseudomonas aeruginosa
phosphorylcholine
-
 Pseudomonas aeruginosa

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ activates, Zn2+ and Cu2+ are better activators than Mg2+ at pH 5.0 Pseudomonas aeruginosa
Mg2+ activates, Zn2+ and Cu2+ are better activators than Mg2+ at pH 5.0 Pseudomonas aeruginosa
Zn2+ activates, Zn2+ and Cu2+ are better activators than Mg2+ at pH 5.0. Zn2+ induces a pH-dependent a conformational change in the active center, at pH 5.0, that is communicated to the inhibitory site, producing a compact or closed structure. However, at pH 7.4, this effect is not observed because to the hydrolysis of the [Zn2+L-12 L02(H2O)2] complex, which causes a change from octahedral to tetrahedral in the metal coordination geometry Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphocholine + H2O Pseudomonas aeruginosa
-
 choline + phosphate
-
 ?
phosphoethanolamine + H2O Pseudomonas aeruginosa
-
 ethanolamine + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q9HTR2 gene pchP, locus PA5292
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein D31 is phosphorylated during phosphoester hydrolysis Pseudomonas aeruginosa

Purification (Commentary)

Purification (Comment) Organism
recombinant PchP from Escherichia coli, as an N-terminal fusion to intein or a histidine tag, in the folded state Pseudomonas aeruginosa

Reaction

Reaction Comment Organism Reaction ID
phosphocholine + H2O = choline + phosphate catalytic mechanism, overview Pseudomonas aeruginosa
a
phosphoethanolamine + H2O = ethanolamine + phosphate catalytic mechanism, overview Pseudomonas aeruginosa
a

Source Tissue

Source Tissue Comment Organism Textmining
additional information growth on choline, betaine, dimethylglycine, or carnitine Pseudomonas aeruginosa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information phosphorylcholine phosphatase catalyzes the hydrolysis of 4-nitrophenylphosphate Pseudomonas aeruginosa ?
-
 ?
phosphocholine + H2O
-
 Pseudomonas aeruginosa choline + phosphate
-
 ?
phosphocholine + H2O substrate docking assay and structure, the oxygen atom of the carboxyl group of D31 is involved in nucleophilic attack on the phosphorus atom of the substrate, the D33 residue is important for catalysis because it participates in the phosphorylation of D31, overview. D262 and D267 are the aspartyl residues involved in catalysis Pseudomonas aeruginosa choline + phosphate
-
 ?
phosphoethanolamine + H2O
-
 Pseudomonas aeruginosa ethanolamine + phosphate
-
 ?
phosphoethanolamine + H2O substrate docking assay and structure, the oxygen atom of the carboxyl group of D31 is involved in nucleophilic attack on the phosphorus atom of the substrate, the D33 residue is important for catalysis because it participates in the phosphorylation of D31, overview. D262 and D267 are the aspartyl residues involved in catalysis Pseudomonas aeruginosa ethanolamine + phosphate
-
 ?

Subunits

Subunits Comment Organism
More the active enzyme is a dimer, enzyme structure molecular modeling and molecular dynamics, with substrate and inhibitor binding sites, overview Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
PChP
-
 Pseudomonas aeruginosa
phosphorylcholine phosphatase
-
 Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 6
-
 Pseudomonas aeruginosa

pH Range

pH Minimum pH Maximum Comment Organism
5 8 optimal range, substrate phosphocholine Pseudomonas aeruginosa

Expression

Organism Comment Expression
Pseudomonas aeruginosa the regulation of pchP gene expression is under the control of GbdR and NtrC additional information
Pseudomonas aeruginosa dimethylglycine is likely the metabolite directly involved in the induction of PchP. Induction of pchP transcription by glycine betaine, a product of choline oxidation, via betaine aldehyde, mediated by GbdR, an AraC family transcription factor up

General Information

General Information Comment Organism
metabolism the regulation of choline metabolism and consequently PchP synthesis may reflect an adaptive response of Pseudomonas aeruginosa to environmental conditions. Regulation of pchP gene expression, overview Pseudomonas aeruginosa