Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity

Protein Engineering, Design and Selection

Volumn 18, Issue 4, 2005, Pages 161-163

  Lassila, Jonathan Kyle ^a   Keeffe, Jennifer R ^a   Oelschlaeger, Peter ^a   Mayo, Stephen L ^a,b  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

^b California Institute of Technology   (United States)

Author keywords

Chorismate mutase; Enzyme design; Protein design

Indexed keywords

CATALYSIS; CATALYSTS; COMPUTATION THEORY; ESCHERICHIA COLI;

CATALYTIC ACTIVITY; CATALYTIC EFFICIENCY; CHORISMATE MUTASE; PROTEIN DESIGN;

ENZYMES;

ALANINE; CHORISMATE MUTASE; SERINE;

ARTICLE; BACTERIUM MUTANT; CALCULATION; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ESCHERICHIA COLI; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL;

ALANINE; AMINO ACID SUBSTITUTION; CATALYSIS; CATALYTIC DOMAIN; CHORISMATE MUTASE; COMPUTATIONAL BIOLOGY; ESCHERICHIA COLI; MUTATION; PROTEIN ENGINEERING; SERINE;

ESCHERICHIA COLI;

EID: 18844410540     PISSN: 17410126     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/gzi015     Document Type: Article

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