Paper Report for: Oda_2021_Methods.Enzymol_648_159
Reference
Title: Cutinases from thermophilic bacteria (actinomycetes): From identification to functional and structural characterization Oda M, Numoto N, Bekker GJ, Kamiya N, Kawai F Ref: Methods Enzymol, 648:159, 2021 : PubMed
Thermophilic cutinases are mainly obtained from thermophilic actinomycetes, and are categorized into two groups, i.e., those with higher (>70 degreesC) or lower (<70 degreesC) thermostabilities. The thermostabilities of cutinases are highly relevant to their ability to degrade polyethylene terephthalate (PET). Many crystal structures of thermophilic cutinases have been solved, showing that their overall backbone structures are identical, irrespective of their ability to hydrolyze PET. One of the unique properties of cutinases is that metal ion-binding on the enzyme's surface both elevates their melting temperatures and activates the enzyme. In this chapter, we introduce the methodology for the identification and cloning of thermophilic cutinases from actinomycetes. For detailed characterization of cutinases, we describe the approach to analyze the intricate dynamics of the enzyme, based on its crystal structures complexed with metal ions and model substrates using a combination of experimental and computational techniques.
        
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Oda M, Numoto N, Bekker GJ, Kamiya N, Kawai F (2021) Cutinases from thermophilic bacteria (actinomycetes): From identification to functional and structural characterization Methods Enzymol648: 159-185
Oda M, Numoto N, Bekker GJ, Kamiya N, Kawai F (2021) Methods Enzymol648: 159-185