A rigidifying salt-bridge favors the activity of thermophilic enzyme at high temperatures at the expense of low-temperature activity

PLoS Biology

Volumn 9, Issue 3, 2011, Pages

  Lam, Sonia Y ^a   Yeung, Rachel C Y ^a   Yu, Tsz Ha ^a   Sze, Kong Hung ^b   Wong, Kam Bo ^a  

^a CHINESE UNIVERSITY OF HONG KONG   (Hong Kong)

^b UNIVERSITY OF HONG KONG   (Hong Kong)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLPHOSPHATASE; ARGININE; CARBOXYL GROUP; ACID ANHYDRIDE HYDROLASE; INORGANIC SALT;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENTHALPY; ENTROPY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME STRUCTURE; HIGH TEMPERATURE; HUMAN; LOW TEMPERATURE; MOLECULAR DYNAMICS; NONHUMAN; PROTEIN MODIFICATION; PYROCOCCUS HORIKOSHII; SIMULATION; CHEMICAL STRUCTURE; CHEMISTRY; COLD; ENZYMOLOGY; GENETICS; HEAT; METABOLISM; PROTEIN CONFORMATION; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

PYROCOCCUS HORIKOSHII;

ACID ANHYDRIDE HYDROLASES; CATALYTIC DOMAIN; COLD TEMPERATURE; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; ENZYME STABILITY; HOT TEMPERATURE; HUMANS; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; PROTEIN CONFORMATION; PYROCOCCUS HORIKOSHII; SALTS; THERMODYNAMICS;

EID: 79953708228     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1001027     Document Type: Article

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