Residues at the Active Site of the Esterase 2 from Alicyclobacillus acidocaldarius Involved in Substrate Specificity and Catalytic Activity at High Temperature

Journal of Biological Chemistry

Volumn 276, Issue 40, 2001, Pages 37482-37490

  Manco, Giuseppe ^a   Mandrich, Luigi ^a   Rossi, Mosè ^a  

^a INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CHEMICAL BONDS; ENZYMES; ESTERS; SUBSTRATES;

ESTER SUBSTRATES;

BIOCHEMISTRY;

4 (2 HYDROXYETHYL) 1 PIPERAZINEETHANESULFONIC ACID; 4 NITROPHENYLBUTANOIC ACID; 4 NITROPHENYLDECANOIC ACID; BACTERIAL ENZYME; CHIMERIC PROTEIN; DECANOIC ACID DERIVATIVE; ENZYME VARIANT; ESTER; ESTERASE; ESTERASE II; M211S PROTEIN; M211S R215L PROTEIN; M211T PROTEIN; M211V PROTEIN; MONOACYLESTER; R215L PROTEIN; UNCLASSIFIED DRUG; CARBOXYLESTERASE;

ALICYCLOBACILLUS ACIDOCALDARIUS; AMINO ACID SUBSTITUTION; ARTICLE; COMPETITIVE INHIBITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HIGH TEMPERATURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ENGINEERING; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; THERMOPHILIC BACTERIUM; BACILLUS; BINDING COMPETITION; BINDING SITE; CATALYSIS; CHEMICAL STRUCTURE; DRUG ANTAGONISM; ENZYMOLOGY; GENETICS; METABOLISM; TEMPERATURE;

ALICYCLOBACILLUS; ALICYCLOBACILLUS ACIDOCALDARIUS; BACTERIA (MICROORGANISMS); FELIS CATUS;

BACILLUS; BINDING SITES; BINDING, COMPETITIVE; CARBOXYLIC ESTER HYDROLASES; CATALYSIS; HEPES; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN ENGINEERING; SUBSTRATE SPECIFICITY; TEMPERATURE;

EID: 0035813133     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M103017200     Document Type: Article

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