PMID:15544334
| Citation |
Del Vecchio, P, Graziano, G, Granata, V, Farias, T, Barone, G, Mandrich, L, Rossi, M and Manco, G (2004) Denaturant-induced unfolding of the acetyl-esterase from Escherichia coli. Biochemistry 43:14637-43 |
|---|---|
| Abstract |
The stability of acetyl-esterase, Aes, from Escherichia coli against the denaturing action of urea and guanidine hydrochloride, GuHCl, has been investigated by means of circular dichroism and fluorescence measurements. The urea-induced unfolding curves show a single inflection point at 6.2 M urea, whereas the GuHCl-induced curves show two inflection points at 1.4 and 3.1 M GuHCl. The unfolding process is reversible with both urea and GuHCl. These results, together with similar experimental data on the mutant form V20D-Aes, suggest the presence of two domains in the Aes structure, which unfold more or less independently depending on the denaturant used. This is also supported by a 3D model obtained by homology modeling using the structure of brefeldine as a template. The effect of NaCl on the urea-induced unfolding curves of the enzyme has also been investigated. |
| Links |
PubMed Online version:10.1021/bi048344f |
| Keywords |
Acetylesterase/chemistry; Acetylesterase/genetics; Aspartic Acid/genetics; Carboxylic Ester Hydrolases/chemistry; Circular Dichroism; Enzyme Stability/genetics; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Guanidine; Models, Molecular; Point Mutation; Protein Denaturation; Protein Folding; Protein Structure, Tertiary/genetics; Sodium Chloride; Spectrometry, Fluorescence; Structural Homology, Protein; Thermodynamics; Urea; Valine/genetics |
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