Evolution of Stability in a Cold-Active Enzyme Elicits Specificity Relaxation and Highlights Substrate-Related Effects on Temperature Adaptation

Journal of Molecular Biology

Volumn 395, Issue 1, 2010, Pages 155-166

  Gatti Lafranconi, Pietro ^a   Natalello, Antonino ^a   Rehm, Sascha ^b   Doglia, Silvia Maria ^a   Pleiss, Jürgen ^b   Lotti, Marina ^a  

^a UNIVERSITY OF MILANO BICOCCA   (Italy)

^b UNIVERSITY OF STUTTGART   (Germany)

Author keywords

circular dichroism; differential scanning fluorimetry; directed evolution; molecular dynamics; temperature adaptation

Indexed keywords

MUTANT PROTEIN; TRIACYLGLYCEROL; TRIACYLGLYCEROL LIPASE;

ARTICLE; CIRCULAR DICHROISM; COLD SENSITIVITY; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVE SITE; ENZYME DENATURATION; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME SUBSTRATE; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; TEMPERATURE ACCLIMATIZATION; TEMPERATURE DEPENDENCE; TEMPERATURE MEASUREMENT; WILD TYPE;

EID: 70450222294     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.10.026     Document Type: Article

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