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Literature summary for 3.11.1.1 extracted from

  • Zhang, G.; Mazurkie, A.S.; Dunaway-Mariano, D.; Allen, K.N.
    Kinetic evidence for a substrate-induced fit in phosphonoacetaldehyde hydrolase catalysis (2002), Biochemistry, 41, 13370-13377.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli JM109 Bacillus cereus

Protein Variants

Protein Variants Comment Organism
K121R/K146R/K192R site-directed mutagenesis, reduced activity compared to the wild-type enzyme Bacillus cereus
K183A site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, Lys183 is probably important in maintaining the active site environment Bacillus cereus
K183L site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, Lys183 is probably important in maintaining the active site environment Bacillus cereus

Inhibitors

Inhibitors Comment Organism Structure
2,4-Dinitrophenylacetate loss of activity due to acetylation of Ls53 with the inert compound, pH profile of inactivation Bacillus cereus
Trypsin degradation Bacillus cereus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Bacillus cereus
0.033
-
phosphonoacetaldehyde wild-type enzyme, pH 7.5, 25°C Bacillus cereus
0.056
-
phosphonoacetaldehyde triple mutant K121R/K146R/K192R, pH 7.5, 25°C Bacillus cereus
0.193
-
phosphonoacetaldehyde mutant K183A, pH 7.5, 25°C Bacillus cereus
0.77
-
phosphonoacetaldehyde mutant K183L, pH 7.5, 25°C Bacillus cereus

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Bacillus cereus O31156
-
-

Reaction

Reaction Comment Organism Reaction ID
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate mechanism, active site conformation during catalysis, Lys53 is involved Bacillus cereus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphonoacetaldehyde + H2O i.e. Pald, cleavage via Schiff base intermediate formed with Lys53, bound substrate stabilizes the closed conformation of the active site, thus facilitating catalysis Bacillus cereus acetaldehyde + phosphate
-
?

Synonyms

Synonyms Comment Organism
2-phosphonoacetaldehyde phosphonohydrolase
-
Bacillus cereus
phosphonatase
-
Bacillus cereus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.012
-
phosphonoacetaldehyde mutant K183A, pH 7.5, 25°C Bacillus cereus
0.046
-
phosphonoacetaldehyde mutant K183L, pH 7.5, 25°C Bacillus cereus
1.28
-
phosphonoacetaldehyde triple mutant K121R/K146R/K192R, pH 7.5, 25°C Bacillus cereus
6.08
-
phosphonoacetaldehyde triple mutant K121R/K146R/K192R, pH 7.5, 25°C Bacillus cereus
15
-
phosphonoacetaldehyde wild-type enzyme, pH 7.5, 25°C Bacillus cereus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information inhibition kinetics Bacillus cereus