Exhaustive mutagenesis of six secondary active-site residues in Escherichia coli chorismate mutase shows the importance of hydrophobic side chains and a helix N-capping position for stability and catalysis

Biochemistry

Volumn 46, Issue 23, 2007, Pages 6883-6891

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

^a California Institute of Technology   (United States)

^b CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

^c ETH ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; ESCHERICHIA COLI; HYDROGEN BONDS; HYDROPHOBICITY; MUTAGENESIS;

COMPUTATIONAL ENZYMES; HYDROPHOBIC SIDE CHAINS; MUTASE-PREPHENATE DEHYDRATASE;

ENZYMES;

AMINO ACID; BACTERIAL ENZYME; CHORISMATE MUTASE; PREPHENATE DEHYDRATASE;

ARTICLE; CATALYSIS; ELECTRICITY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STABILITY; ESCHERICHIA COLI; HYDROGEN BOND; HYDROPHOBICITY; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BINDING SITES; CATALYSIS; CHORISMATE MUTASE; ENZYME STABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT;

ESCHERICHIA COLI;

EID: 34250156703     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700215x     Document Type: Article

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