A mixed mechanistic-electrostatic model to explain pH dependence of glycosyl hydrolase enzyme activity

Biotechnology and Bioengineering

Volumn 86, Issue 5, 2004, Pages 573-586

  Olivera Nappa, Alvaro ^a   Andrews, Barbara A ^a   Asenjo, Juan A ^a  

^a UNIVERSITY OF CHILE   (Chile)

Author keywords

Enzyme activity; Glycoside hydrolases; Hydrogen bonding network; Mathematical model; Mutagenesis; pH dependence; Protein engineering

Indexed keywords

DISSOCIATION; ELECTROSTATICS; ENVIRONMENTAL IMPACT; ENZYMES; HYDROGEN BONDS; PH EFFECTS;

ACIDIC RESIDUES; ELECTROSTATIC INTERACTIONS;

BIOTECHNOLOGY;

GLYCOSIDASE;

ARTICLE; CHEMICAL MODIFICATION; ELECTRICITY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; EQUILIBRIUM CONSTANT; HYDROGEN BOND; MATHEMATICAL MODEL; MOLECULAR INTERACTION; MUTAGENESIS; PROTEIN ENGINEERING; SITE DIRECTED MUTAGENESIS;

CATALYSIS; COMPUTER SIMULATION; ELECTROSTATICS; ENZYME ACTIVATION; ENZYME STABILITY; GLYCOSIDE HYDROLASES; HYDROGEN-ION CONCENTRATION; KINETICS; MECHANICS; MODELS, CHEMICAL; MODELS, MOLECULAR; PROTEIN CONFORMATION;

EID: 2542490268     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.20063     Document Type: Article

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