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Literature summary for 3.1.3.75 extracted from

  • Beassoni, P.R.; Otero, L.H.; Boetsch, C.; Domenech, C.E.; Gonzalez-Nilo, F.D.; Lisa, A.T.
    Site-directed mutations and kinetic studies show key residues involved in alkylammonium interactions and reveal two sites for phosphorylcholine in Pseudomonas aeruginosa phosphorylcholine phosphatase (2011), Biochim. Biophys. Acta, 1814, 858-863.
    View publication on PubMed
Search for more literature for 3.1.3.75

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21 Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
E42A site-directed mutagenesis Pseudomonas aeruginosa
E43A site-directed mutagenesis Pseudomonas aeruginosa
Y82A/Y83A/Y84A site-directed mutagenesis Pseudomonas aeruginosa

Inhibitors

Inhibitors Comment Organism Structure
phosphocholine substrate inhibition at high concentration Pseudomonas aeruginosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.51
-
 4-nitrophenyl phosphate pH 5.0, 37°C, recombinant mutant Y82A/Y83A/Y84A Pseudomonas aeruginosa
0.56
-
 4-nitrophenyl phosphate pH 5.0, 37°C, recombinant mutant E43A Pseudomonas aeruginosa
1.5 2 4-nitrophenyl phosphate pH 5.0, 37°C, recombinant wild-type enzyme Pseudomonas aeruginosa
1.9
-
 4-nitrophenyl phosphate pH 5.0, 37°C, recombinant mutant E42A Pseudomonas aeruginosa

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on 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
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
10.1
-
 purified recombinant mutant Y82A/Y83A/Y84A, pH 5.0, 37°C, substrate 4-nitrophenyl phosphate Pseudomonas aeruginosa
59
-
 purified recombinant mutant E42A, pH 5.0, 37°C, substrate 4-nitrophenyl phosphate Pseudomonas aeruginosa
121
-
 purified recombinant mutant E43A, pH 5.0, 37°C, substrate 4-nitrophenyl phosphate Pseudomonas aeruginosa
132.7
-
 purified recombinant wild-type enzyme, pH 5.0, 37°C, substrate 4-nitrophenyl phosphate Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
 Pseudomonas aeruginosa 4-nitrophenol + phosphate
-
 ?
phosphocholine + H2O
-
 Pseudomonas aeruginosa choline + phosphate
-
 ?
phosphoethanolamine + H2O
-
 Pseudomonas aeruginosa ethanolamine + phosphate
-
 ?

Subunits

Subunits Comment Organism
More the enzyme contains three HAD motifs, sequence comparisons, overview Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the haloacid dehalogenase superfamily Pseudomonas aeruginosa
PChP
-
 Pseudomonas aeruginosa
phosphoethanolamine/phosphocholine phosphatase
-
 Pseudomonas aeruginosa
phosphorylcholine phosphatase
-
 Pseudomonas aeruginosa

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.7
-
 4-nitrophenyl phosphate pH 5.0, 37°C, recombinant mutant Y82A/Y83A/Y84A Pseudomonas aeruginosa
38.8
-
 4-nitrophenyl phosphate pH 5.0, 37°C, recombinant mutant E42A Pseudomonas aeruginosa
79.6
-
 4-nitrophenyl phosphate pH 5.0, 37°C, recombinant mutant E43A Pseudomonas aeruginosa
87.1
-
 4-nitrophenyl phosphate pH 5.0, 37°C, recombinant wild-type enzyme Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 assay at Pseudomonas aeruginosa

General Information

General Information Comment Organism
additional information combination of molecular modeling, directed mutagenesis and enzyme kinetics to study the mode of interaction of PchP phosphatase with the choline moiety of the substrate Pseudomonas aeruginosa

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
13.3
-
 4-nitrophenyl phosphate purified recombinant mutant Y82A/Y83A/Y84A, pH 5.0, 37°C Pseudomonas aeruginosa
21.4
-
 4-nitrophenyl phosphate purified recombinant mutant E42A, pH 5.0, 37°C Pseudomonas aeruginosa
57.2
-
 4-nitrophenyl phosphate purified recombinant wild-type enzyme, pH 5.0, 37°C Pseudomonas aeruginosa
141
-
 4-nitrophenyl phosphate purified recombinant mutant E43A, pH 5.0, 37°C Pseudomonas aeruginosa