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Structure and dynamics of cold-adapted enzymes as investigated by FT-IR spectroscopy and MD. the case of an esterase from Pseudoalteromonas haloplanktis

Journal of Physical Chemistry B, ISSN: 1520-6106, Vol: 113, Issue: 22, Page: 7753-7761
2009
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Article Description

Psychrophiles are cold-adapted organisms that produce enzymes that display a high catalytic efficiency at low temperatures. In recent years, these low-temperature working enzymes have attracted the attention of scientists because of their peculiar properties that render them particularly useful in investigating the relationship between enzyme stability and flexibility. Recently, a new esterase was identified and isolated from the coldadapted organism Pseudoalteromonas haloplanktis. The enzyme, denoted as PhEST, presents a dimeric structure with a molecular mass of 60 kDa. In this work, we used Fourier transform infrared spectroscopy and molecular dynamics simulations to investigate the functional and structural properties of PhEST over a wide range of temperature. The obtained results reveal that the structure of PhEST is quite stable up to 40 °C. In fact, the protein starts to denature at about 45 °C through the formation of new secondary structural elements such as intermolecular β-sheets. In addition, our results indicate that the flexibility of protein segment 55-65 (335-345 in subunit B), which corresponds to a loop near the active site of the enzyme, plays a crucial role in the protein function. © 2009 American Chemical Society.

Bibliographic Details

Aurilia, Vincenzo; Rioux-Dubé, Jean-François; Marabotti, Anna; Pézolet, Michel; D'Auria, Sabato

American Chemical Society (ACS)

Chemistry; Materials Science

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