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Literature summary extracted from

  • Kim, A.; Benning, M.M.; OkLee, S.; Quinn, J.; Martin, B.M.; Holden, H.M.; Dunaway-Mariano, D.
    Divergence of chemical function in the alkaline phosphatase superfamily: structure and mechanism of the P-C bond cleaving enzyme phosphonoacetate hydrolase (2011), Biochemistry, 50, 3481-3494.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.11.1.2 Phosphonoacetate substrate activation, mechanism, overview Pseudomonas fluorescens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.11.1.2 recombinant expression in Escherichia coli strain JM105 Pseudomonas fluorescens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.11.1.2 purified recombinant enzyme in in the presence of Zn2+, Mg2+, phosphonoformate and tartrate, from 30 mM K+BICINE, pH 8.5, and 1 mM ZnCl2, mixed with 10% poly(ethylene glycol) 8000, 100 mM Mg-acetate, and 5 mM phosphonoformate buffered at pH 7.0 with 100 mM MOPSO, X-ray diffraction structure determination and analysis at 2.8 A resolution, multiple isomorphous replacement with two heavy-atom derivatives Pseudomonas fluorescens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.11.1.2 Phosphonoformate competitive inhibitor, the phosphonoformate ligand and two zinc ions are bound at the core domain Pseudomonas fluorescens
3.11.1.2 phosphonoproprionate competitive inhibitor Pseudomonas fluorescens
3.11.1.2 Phosphonopyruvate competitive inhibitor Pseudomonas fluorescens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.11.1.2 Co2+ activates 2fold at 3 mM Pseudomonas fluorescens
3.11.1.2 additional information no effects by Mg2+, Ca2+, Ni2+, Mn2+, Cr2+, Cu2+ at 3 mM Pseudomonas fluorescens
3.11.1.2 Zn2+ activates 10fold at 3 mM, the phosphonoformate ligand and two zinc ions are bound at the core domain Pseudomonas fluorescens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.11.1.2 44239
-
 2 * 44239, sequence calculation and gel filtration Pseudomonas fluorescens
3.11.1.2 93000
-
 gel filtration, recombinant enzyme Pseudomonas fluorescens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.11.1.2 Phosphonoacetate + H2O Pseudomonas fluorescens
-
 acetate + phosphate
-
 ?
3.11.1.2 Phosphonoacetate + H2O Pseudomonas fluorescens 23F
-
 acetate + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.11.1.2 Pseudomonas fluorescens
-
-
-
3.11.1.2 Pseudomonas fluorescens 23F
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.11.1.2 recombinant enzyme from Escherichia coli strain JM105 by ammonium sulfate fractionation, and anion exchange, hydrophobic interaction, and hydroxylapatite chromatography, followed by gel filtration Pseudomonas fluorescens

Reaction

EC Number Reaction Comment Organism Reaction ID
3.11.1.2 Phosphonoacetate + H2O = acetate + phosphate structure and mechanism of the P-C bond cleaving enzyme, nucleophilic catalysis involving a zinc ion, overview. Modeling of the catalytic mechanism Pseudomonas fluorescens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.11.1.2 additional information substrate specificity, overview. No activity with fosfomycin or phosphonopyruvate Pseudomonas fluorescens ?
-
 ?
3.11.1.2 additional information substrate specificity, overview. No activity with fosfomycin or phosphonopyruvate Pseudomonas fluorescens 23F ?
-
 ?
3.11.1.2 Phosphonoacetate + H2O
-
 Pseudomonas fluorescens acetate + phosphate
-
 ?
3.11.1.2 Phosphonoacetate + H2O
-
 Pseudomonas fluorescens 23F acetate + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.11.1.2 homodimer 2 * 44239, sequence calculation and gel filtration Pseudomonas fluorescens
3.11.1.2 More PAc hydrolase monomer is comprised of a large alpha/beta/alpha core domain of residues 1-245 and 367-388, 6-stranded mixed beta-sheet, and a smaller alpha/beta cap domain comprising residues 255-360, as 4-stranded antiparallel beta-sheet Pseudomonas fluorescens

Synonyms

EC Number Synonyms Comment Organism
3.11.1.2 PAc hydrolase
-
 Pseudomonas fluorescens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.11.1.2 25 30 assay at Pseudomonas fluorescens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.11.1.2 7 8 assay at Pseudomonas fluorescens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.11.1.2 0.049
-
 Phosphonoformate pH 7.0, 25°C Pseudomonas fluorescens
3.11.1.2 0.19
-
 Phosphonoformate pH 7.0, 30°C Pseudomonas fluorescens
3.11.1.2 1.2
-
 Phosphonopyruvate pH 7.0, 30°C Pseudomonas fluorescens
3.11.1.2 1.2
-
 phosphonoproprionate pH 7.0, 30°C Pseudomonas fluorescens

General Information

EC Number General Information Comment Organism
3.11.1.2 evolution the P-C bond cleaving enzyme phosphonoacetate hydrolase belongs to the alkaline phosphatase superfamily Pseudomonas fluorescens
3.11.1.2 metabolism the enzyme is involved in the 2-aminoethylphosphonic acid degradation pathway, overview Pseudomonas fluorescens