Comparative thermostability of mesophilic and thermophilic alcohol dehydrogenases: Stability-determining roles of proline residues and loop conformations

Enzyme and Microbial Technology

Volumn 45, Issue 2, 2009, Pages 73-79

  Barzegar, Abolfazl ^a,b   Moosavi Movahedi, Ali A ^a   Pedersen, Jens Z ^c   Miroliaei, Mehran ^d  

^a UNIVERSITY OF TEHRAN   (Iran)

^b UNIVERSITY OF TABRIZ   (Iran)

^c UNIVERSITY OF ROME TOR VERGATA   (Italy)

^d UNIVERSITY OF ISFAHAN   (Iran)

Author keywords

Mesophilic ADHs; Multimeric proteins; Proline; Thermal inactivation; Thermophilic ADH; Thermostability

Indexed keywords

MESOPHILIC ADHS; MULTIMERIC PROTEINS; PROLINE; THERMAL INACTIVATION; THERMOPHILIC ADH; THERMOSTABILITY;

ACTIVATION ENERGY; ALIGNMENT; CATALYSTS;

ENZYMES;

ALCOHOL DEHYDROGENASE; PROLINE;

AMINO ACID SEQUENCE; ARTICLE; COMPARATIVE STUDY; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME CONFORMATION; MESOPHILE; RIGIDITY; TEMPERATURE STRESS; THERMOPHILIC BACTERIUM; THERMOSTABILITY; X RAY ANALYSIS;

EQUIDAE; THERMOANAEROBACTER BROCKII;

EID: 67549134221     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2009.04.007     Document Type: Article

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