Thermostability and thermoactivity of enzymes from hyperthermophilic archaea
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2020, Journal of Structural BiologyCitation Excerpt :The enzyme activity has been well described in terms of kinetics parameters, substrate specificity and folding in the hyperthermophilic Archaea Sulfolobus solfataricus (Porcelli et al., 1988; Wang et al., 2014), Methanococcus jannaschii (Garrido et al., 2009; Lu and Markham, 2002) and Thermococcus kodakarensis (Schlesier et al., 2013). Hyperthermophilic Archaea are worthy of attention and have been the subject of intense research over the years not only for their exceptional stability but also for their peculiar physicochemical characteristics that have led to many biotechnological applications (Adams and Kelly, 1994; Niehaus et al., 1999; Vieille and Zeikus, 2001). These enzymes, indeed, provide unique models for the study of the evolution of enzymes in terms of structure, stability, substrate specificity, catalytic properties and mechanism of action.
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