Role of the N terminus in enzyme activity, stability and specificity in thermophilic esterases belonging to the HSL family

Journal of Molecular Biology

Volumn 345, Issue 3, 2005, Pages 501-512

  Mandrich, Luigi ^a   Merone, Luigia ^a   Pezzullo, Margherita ^a   Cipolla, Laura ^b   Nicotra, Francesco ^b   Rossi, Mosè ^a   Manco, Giuseppe ^a  

^a CNR   (Italy)

^b UNIVERSITY OF MILANO BICOCCA   (Italy)

Author keywords

"cap" domain; HSL family; N terminus; substrate specificity; thermophilic carboxylesterase

Indexed keywords

CAP BINDING PROTEIN; DECANOIC ACID DERIVATIVE; ESTERASE; HEXANOIC ACID; THIOL ESTER HYDROLASE; TRIACYLGLYCEROL;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STABILITY; ESCHERICHIA COLI; GENE DELETION; GENETIC CODE; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SULFOLOBUS SOLFATARICUS; THERMOPHILIC BACTERIUM;

ALICYCLOBACILLUS ACIDOCALDARIUS; BURKHOLDERIA; BURKHOLDERIA CEPACIA; ESCHERICHIA COLI; SULFOLOBUS SOLFATARICUS;

EID: 9644275365     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.10.035     Document Type: Article

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