Publications by authors named "E A Lampitella"

The human paraoxonase 2 (PON2) is the oldest member of a small family of arylesterase and lactonase enzymes, representing the first line of defense against bacterial infections and having a major role in ROS-associated diseases such as cancer, cardiovascular diseases, neurodegeneration, and diabetes. Specific Post-Translational Modifications (PTMs) clustering nearby two residues corresponding to polymorphic sites and their impact on the catalytic activity are not yet fully understood. Thus, the goal of the present study was to develop an improved PON2 purification protocol to obtain a higher amount of protein suitable for in-depth biochemical studies and biotechnological applications.

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The problem of biofilm formation is a serious concern under various pathological conditions such as extensive burns, wounds in diabetic patients, bedsores, cystic fibrosis, nosocomial infections from implantable medical devices such as catheters, valves, etc. Environmental diffusion of biofilm (in pools, wet floors, industrial food plants) that could represent a reservoir of antibiotic resistant bacteria constitues an additional issue. In this work is described a lactonase from Rhodococcus erythropolis, a phosphotriesterase-like lactonase (PLL) enzyme, which has already been studied in the past and can be used for containment of biofilm formation.

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Article Synopsis
  • Ageritin is a protein from edible mushrooms that functions as a ribotoxin and requires zinc ions for its enzymatic activity, which involves breaking specific bonds in ribosomes.
  • Research on ageritin's stability across different pH levels showed it has high thermal stability with a denaturation temperature of 78°C and a Gibbs energy value of 36 kJ/mol at pH 5.0.
  • The study also looked at a modified form of ageritin where a specific cysteine was altered; although this form maintained enzymatic activity, it demonstrated lower stability and highlighted the significance of zinc in maintaining the protein's structure.
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Ageritin is the prototype of a new ribotoxin-like protein family, which has been recently identified also in basidiomycetes. The protein exhibits specific RNase activity through the cleavage of a single phosphodiester bond located at sarcin/ricin loop of the large rRNA, thus inhibiting protein biosynthesis at early stages. Conversely to other ribotoxins, its activity requires the presence of divalent cations.

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