Functional and structural features of the oxyanion hole in a thermophilic esterase from Alicyclobacillus acidocaldarius

Proteins: Structure, Function and Genetics

Volumn 71, Issue 4, 2008, Pages 1721-1731

  Mandrich, Luigi ^a   Menchise, Valeria ^b,c   Alterio, Vincenzo ^b   De Simone, Giuseppina ^b   Pedone, Carlo ^b,d   Rossi, Mosè ^a   Manco, Giuseppe ^a  

^a INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

^b CNR   (Italy)

^c Bioindustry Park del Canavese   (Italy)

^d UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

Carboxylesterase; Oxyanion loop; pH activity profile; Reaction mechanism; Thermophilicity

Indexed keywords

4 (2 HYDROXYETHYL) 1 PIPERAZINEETHANESULFONIC ACID; ESTERASE; MUTANT PROTEIN;

ALICYCLOBACILLUS ACIDOCALDARIUS; ARTICLE; CATALYSIS; HYDROGEN BOND; MOLECULAR MECHANICS; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; TEMPERATURE; THERMOSTABILITY; THREE DIMENSIONAL IMAGING;

BACILLUS; BINDING SITES; CARBOXYLIC ESTER HYDROLASES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; GLYCINE; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SERINE; SUBSTRATE SPECIFICITY; TEMPERATURE; WATER; X-RAY DIFFRACTION;

ALICYCLOBACILLUS ACIDOCALDARIUS;

EID: 44349174350     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21877     Document Type: Article

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