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Literature summary for 3.1.1.6 extracted from

  • Del Vecchio, P.; Graziano, G.; Barone, G.; Mandrich, L.; Rossi, M.; Manco, G.
    Temperature-induced denaturation of Aes acetyl-esterase from Escherichia coli (2006), Thermochim. Acta, 441, 144-149.
No PubMed abstract available
Search for more literature for 3.1.1.6

Cloned(Commentary)

Cloned (Comment) Organism
gene ybaC, overexpression of wild-type and mutant enzymes Escherichia coli

Protein Variants

Protein Variants Comment Organism
V20D site-directed mutagenesis, the mutant shows slightly reduced thermal stability compared to the wild-type enzyme, kinetic analysis, overview Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 gene ybaC
-

Synonyms

Synonyms Comment Organism
acetyl-esterase
-
 Escherichia coli
Aes
-
 Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
61
-
 denaturation of Aes mutant V20D, thermal stability analysis at 20-90°C, differential scanning calorimetry and circular dichroism measurements, the irreversible inactivation process is more complex than a two-state transition Escherichia coli
68
-
 denaturation of Aes, thermal stability analysis at 20-90°C, differential scanning calorimetry and circular dichroism measurements, the irreversible inactivation process is more complex than a two-state transition Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli