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Literature summary for 3.1.1.6 extracted from

  • Kobayashi, R.; Hirano, N.; Kanaya, S.; Haruki, M.
    Enhancement of the enzymatic activity of Escherichia coli acetyl esterase by a double mutation obtained by random mutagenesis (2012), Biosci. Biotechnol. Biochem., 76, 2082-2088.
    View publication on PubMed
Search for more literature for 3.1.1.6

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli JM109 cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
L209F the mutant shows 3.8fold increased activity compared to the wild type enzyme Escherichia coli
L97F the mutant shows 5.4fold increased activity compared to the wild type enzyme Escherichia coli
L97F/L209F the mutant shows 28.8fold increased activity compared to the wild type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.057
-
 4-nitrophenyl butyrate mutant enzyme L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C Escherichia coli
0.069
-
 4-nitrophenyl butyrate mutant enzyme L97F/L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C Escherichia coli
0.17
-
 4-nitrophenyl butyrate wild type enzyme, in 20 mM phosphate buffer, at pH 7.1 and 30°C Escherichia coli
0.26
-
 4-nitrophenyl butyrate mutant enzyme L97F, in 20 mM phosphate buffer, at pH 7.1 and 30°C Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 x * 40000, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl butyrate + H2O
-
 Escherichia coli 4-nitrophenol + butyrate
-
 ?

Subunits

Subunits Comment Organism
? x * 40000, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
Acetyl esterase
-
 Escherichia coli
Est1
-
 Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
 the wild type enzyme shows a half-life of 40 min at 55°C Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
29
-
 4-nitrophenyl butyrate wild type enzyme, in 20 mM phosphate buffer, at pH 7.1 and 30°C Escherichia coli
37
-
 4-nitrophenyl butyrate mutant enzyme L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C Escherichia coli
240
-
 4-nitrophenyl butyrate mutant enzyme L97F, in 20 mM phosphate buffer, at pH 7.1 and 30°C Escherichia coli
340
-
 4-nitrophenyl butyrate mutant enzyme L97F/L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.057
-
 4-nitrophenyl butyrate mutant enzyme L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C Escherichia coli
0.069
-
 4-nitrophenyl butyrate mutant enzyme L97F/L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C Escherichia coli
0.17
-
 4-nitrophenyl butyrate wild type enzyme, in 20 mM phosphate buffer, at pH 7.1 and 30°C Escherichia coli
0.26
-
 4-nitrophenyl butyrate mutant enzyme L97F, in 20 mM phosphate buffer, at pH 7.1 and 30°C Escherichia coli