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Biochemical and Thermostability Features of Acetyl Esterase Aes from Escherichia coli

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Previously we characterized an acetyl-esterase from Escherichia coli, formally Aes, from a thermodynamic point of view in comparative studies with thermophilic homologs. Since the enzyme appeared unusually resistant to the thermal denaturation we analysed the kinetic behaviour with respect to the temperature. The enzyme displays a surprising optimal temperature at 65 °C, showing a specific activity of 250 U/mg using pNP-butanoate as substrate, but a low kinetic stability at the same temperature (t1/2 of inactivation=5 min). By a random mutagenesis approach we searched for mutated versions of Aes with increased thermostability. We found the mutant T74A, which shows the same specific activity of wild type but a t1/2 of inactivation of 30 min at 65 °C.

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Keywords: Aes; HSL family; Hormone Sensitive lipase family of the esterase/lipase superfamily; SDS-PAGE; acetyl-esterase from Escherichia coli; sodium dodecyl sulfate-polyacrylamide gel electrophoresis

Document Type: Research Article

Affiliations: Istituto di Biochimica delle Proteine, Consiglio Nazionale delle Ricerche (CNR), Via Pietro Castellino 111, 80131 Naples, Italy.

Publication date: February 1, 2007

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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