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Literature summary extracted from

  • Morais, M.C.; Zhang, G.; Zhang, W.; Olsen, D.B.; Dunaway-Mariano, D.; Allen, K.N.
    X-ray crystallographic and site-directed mutagenesis analysis of the mechanism of Schiff-base formation in phosphonoacetaldehyde hydrolase catalysis (2004), J. Biol. Chem., 279, 9353-9361.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.11.1.1 expression of wild-type and mutant enzymes in Escherichia coli Bacillus cereus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.11.1.1 10 mg/ml purified recombinant wild-type and mutant enzymes, complexed with Mg2+ only or with Mg2+ and inhibitor vinyl sulfonate, in 1 mM HEPES, 10 mM MgCl2, 0.1 mM DTT, pH 7.5, 4°C, hanging drop vapour diffusion method, equal volume of protein and reservoir solution, the latter containing 30% PEG 4000, 100 mM Tris-HCl, pH 7.4, 100 mM MgCl2, 1 week, against the reservoir well solution additionally with 20% glycerol before data collection, X-ray diffraction structure determination and analysis at 2.4-2.8 A resolution Bacillus cereus

Protein Variants

EC Number Protein Variants Comment Organism
3.11.1.1 C22A site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Bacillus cereus
3.11.1.1 C22S site-directed mutagenesis, reduced activity compared to the wild-type enzyme Bacillus cereus
3.11.1.1 H56A site-directed mutagenesis, very highly reduced activity compared to the wild-type enzyme Bacillus cereus
3.11.1.1 M49L site-directed mutagenesis, very highly reduced activity compared to the wild-type enzyme Bacillus cereus
3.11.1.1 Y128A site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme Bacillus cereus
3.11.1.1 Y128F site-directed mutagenesis, reduced activity compared to the wild-type enzyme Bacillus cereus
3.11.1.1 Y128F/C22S site-directed mutagenesis, reduced activity compared to the wild-type enzyme Bacillus cereus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.11.1.1 vinyl sulfonate competitive, inhibition mechanism Bacillus cereus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.11.1.1 0.033
-
 phosphonoacetaldehyde wild-type enzyme, mutant C22S, and mutant Y128F/C22S, pH 7.5, 25°C Bacillus cereus
3.11.1.1 0.035
-
 phosphonoacetaldehyde mutant Y128A, pH 7.5, 25°C Bacillus cereus
3.11.1.1 0.045
-
 phosphonoacetaldehyde mutant Y128F, pH 7.5, 25°C Bacillus cereus
3.11.1.1 0.145
-
 phosphonoacetaldehyde mutant H56A, pH 7.5, 25°C Bacillus cereus
3.11.1.1 0.53
-
 phosphonoacetaldehyde mutant C22A, pH 7.5, 25°C Bacillus cereus
3.11.1.1 5.1
-
 phosphonoacetaldehyde mutant M49L, pH 7.5, 25°C Bacillus cereus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.11.1.1 Mg2+ required for catalysis Bacillus cereus

Organism

EC Number Organism UniProt Comment Textmining
3.11.1.1 Bacillus cereus O31156
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.11.1.1 recombinant wild-type and mutant enzymes from Escherichia coli Bacillus cereus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.11.1.1 phosphonoacetaldehyde + H2O = acetaldehyde + phosphate mechanism, reaction pathway, Schiff base formation between an amine and a ketone in aqueous solution, active site model Bacillus cereus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.11.1.1 phosphonoacetaldehyde + H2O i.e. Pald Bacillus cereus acetaldehyde + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.11.1.1 phosphonatase
-
 Bacillus cereus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.11.1.1 25
-
 assay at Bacillus cereus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.11.1.1 0.075
-
 phosphonoacetaldehyde mutant H56A, pH 7.5, 25°C Bacillus cereus
3.11.1.1 0.077
-
 phosphonoacetaldehyde mutant Y128A, pH 7.5, 25°C Bacillus cereus
3.11.1.1 1.95
-
 phosphonoacetaldehyde mutant C22A, pH 7.5, 25°C Bacillus cereus
3.11.1.1 2.11
-
 phosphonoacetaldehyde mutant Y128F/C22S, pH 7.5, 25°C Bacillus cereus
3.11.1.1 2.21
-
 phosphonoacetaldehyde mutant Y128F, pH 7.5, 25°C Bacillus cereus
3.11.1.1 2.26
-
 phosphonoacetaldehyde mutant C22S, pH 7.5, 25°C Bacillus cereus
3.11.1.1 2.94
-
 phosphonoacetaldehyde mutant C22S, pH 7.5, 25°C Bacillus cereus
3.11.1.1 2.94
-
 phosphonoacetaldehyde mutant Y128F, pH 7.5, 25°C Bacillus cereus
3.11.1.1 2.94
-
 phosphonoacetaldehyde mutant Y128F/C22S, pH 7.5, 25°C Bacillus cereus
3.11.1.1 15
-
 phosphonoacetaldehyde wild-type enzyme and mutant M49L, pH 7.5, 25°C Bacillus cereus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.11.1.1 7.5
-
 assay at Bacillus cereus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.11.1.1 1.79
-
 vinyl sulfonate pH 7.5, 25°C Bacillus cereus