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Literature summary extracted from

  • Yep, A.; Kenyon, G.L.; McLeish, M.J.
    Saturation mutagenesis of putative catalytic residues of benzoylformate decarboxylase provides a challenge to the accepted mechanism (2008), Proc. Natl. Acad. Sci. USA, 105, 5733-5738.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.7 expressed in Escherichia coli BL21(DE3) cells Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.7 H281A mutant with 152fold decreased kcat value compared to the wild type enzyme Pseudomonas putida
4.1.1.7 H281F mutant with 4.9fold decrease in kcat value compared to the wild type enzyme Pseudomonas putida
4.1.1.7 H281N mutant with 17fold decrease in kcat value compared to the wild type enzyme Pseudomonas putida
4.1.1.7 H281Q mutant with 37fold decrease in kcat value compared to the wild type enzyme Pseudomonas putida
4.1.1.7 H281T mutant with 159fold decrease in kcat value compared to the wild type enzyme Pseudomonas putida
4.1.1.7 H281W mutant with 19fold decrease in kcat value compared to the wild type enzyme Pseudomonas putida
4.1.1.7 H281Y mutant with 46fold decrease in kcat value compared to the wild type enzyme Pseudomonas putida
4.1.1.7 H70A mutant exhibits 4000fold decreased catalytic activity compared to the wild type enzyme Pseudomonas putida
4.1.1.7 H70F mutant exhibits a 236fold decrease in kcat/Km compared to the wild type enzyme Pseudomonas putida
4.1.1.7 H70L mutant exhibits a 33fold decrease in kcat/Km compared to the wild type enzyme Pseudomonas putida
4.1.1.7 H70S mutant exhibits a 197fold decrease in kcat/Km compared to the wild type enzyme Pseudomonas putida
4.1.1.7 H70T mutant exhibits a 25fold decrease in kcat/Km compared to the wild type enzyme Pseudomonas putida
4.1.1.7 S26A mutant with 21fold decrease in kcat value compared to the wild type enzyme Pseudomonas putida
4.1.1.7 S26L mutant exhibits no significant loss of activity compared to the wild type enzyme (2fold decrease in kcat value) Pseudomonas putida
4.1.1.7 S26M mutant exhibits no significant loss of activity compared to the wild type enzyme (12fold decrease in kcat value) Pseudomonas putida
4.1.1.7 S26T mutant exhibits no significant loss of activity compared to the wild type enzyme (3fold decrease in kcat value) Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.7 0.27
-
 benzoylformate wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 0.29
-
 benzoylformate mutant enzyme H281Q, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 0.29
-
 benzoylformate mutant enzyme H281W, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 0.38
-
 benzoylformate mutant enzyme H70L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 0.49
-
 benzoylformate mutant enzyme H281Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 0.54
-
 benzoylformate mutant enzyme H281F, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 0.8
-
 benzoylformate mutant enzyme S26M, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 0.85
-
 benzoylformate mutant enzyme H70F, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 0.85
-
 benzoylformate mutant enzyme S26T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 0.89
-
 benzoylformate mutant enzyme H70T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 0.9
-
 benzoylformate mutant enzyme H281T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 0.94
-
 benzoylformate mutant enzyme H70S, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 1.2
-
 benzoylformate mutant enzyme H281A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 1.2
-
 benzoylformate mutant enzyme S26L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 1.5
-
 benzoylformate mutant enzyme H70A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 2.9
-
 benzoylformate mutant enzyme H281N in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 7.8
-
 benzoylformate mutant enzyme S26A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.7 Pseudomonas putida P20906
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.7
-
 Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.7 benzoylformate
-
 Pseudomonas putida benzaldehyde + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.7 BFDC
-
 Pseudomonas putida

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.7 0.46
-
 benzoylformate mutant enzyme H70A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 2
-
 benzoylformate mutant enzyme H281T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 2.1
-
 benzoylformate mutant enzyme H281A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 4.5
-
 benzoylformate mutant enzyme H70F, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 5.6
-
 benzoylformate mutant enzyme H70S, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 6.9
-
 benzoylformate mutant enzyme H281Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 8.6
-
 benzoylformate mutant enzyme H281Q, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 14
-
 benzoylformate mutant enzyme H70L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 15
-
 benzoylformate mutant enzyme S26A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 17
-
 benzoylformate mutant enzyme H281W, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 19
-
 benzoylformate mutant enzyme H281N in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 26
-
 benzoylformate mutant enzyme S26M, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 42
-
 benzoylformate mutant enzyme H70T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 65
-
 benzoylformate mutant enzyme H281F, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 94
-
 benzoylformate mutant enzyme S26T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 132
-
 benzoylformate mutant enzyme S26L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida
4.1.1.7 320
-
 benzoylformate wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.7 thiamine diphosphate 0.5 mM, required for activity Pseudomonas putida