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Literature summary extracted from

  • Lahiri, S.D.; Zhang, G.; Dai, J.; Dunaway-Mariano, D.; Allen, K.N.
    Analysis of the substrate specificity loop of the HAD superfamily cap domain (2004), Biochemistry, 43, 2812-2820.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.11.1.1 mutant enzymes Bacillus cereus

Protein Variants

EC Number Protein Variants Comment Organism
3.11.1.1 G50A kcat/Km is 12820fold lower than wild-type value Bacillus cereus
3.11.1.1 G50P inactive mutant protein Bacillus cereus
3.11.1.1 G50V inactive mutant protein Bacillus cereus
3.11.1.1 H56Q kcat/Km is 238fold lower than wild-type value Bacillus cereus
3.11.1.1 K53A inactive mutant protein Bacillus cereus
3.11.1.1 K53R inactive mutant protein Bacillus cereus
3.11.1.1 M49L kcat/Km is 17241fold lower than wild-type value 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 25°C, pH 7.5, wild-type enzyme Bacillus cereus
3.11.1.1 0.175
-
 phosphonoacetaldehyde 25°C, pH 7.5, mutant enzyme H56Q Bacillus cereus
3.11.1.1 5.1
-
 phosphonoacetaldehyde 25°C, pH 7.5, mutant enzyme m49L Bacillus cereus
3.11.1.1 11
-
 phosphonoacetaldehyde 25°C, pH 7.5, mutant enzyme G50A Bacillus cereus

Organism

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

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.11.1.1 expression of mutant enzymes in escherichia coli Bacillus cereus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.11.1.1 phosphonoacetaldehyde + H2O catalysis within the core domain of phosphonatase requires the participation of loop 5 of the corresponding cap domain. Gly is an indispensable component Bacillus cereus acetaldehyde + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.11.1.1 phosphonatase
-
 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 0.00247
-
 phosphonoacetaldehyde 25°C, pH 7.5, mutant enzyme m49L Bacillus cereus
3.11.1.1 0.006
-
 phosphonoacetaldehyde 25°C, pH 7.5, mutant enzyme H56Q Bacillus cereus
3.11.1.1 0.0071
-
 phosphonoacetaldehyde 25°C, pH 7.5, mutant enzyme G50A Bacillus cereus
3.11.1.1 0.25
-
 phosphonoacetaldehyde 25°C, pH 7.5, wild-type enzyme Bacillus cereus