Probing the catalytic mechanism of prephenate dehydratase by site- directed mutagenesis of the Escherichia coli P-protein dehydratase domain

Biochemistry

Volumn 39, Issue 16, 2000, Pages 4722-4728

  Zhang, Sheng ^a   Wilson, David B ^a   Ganem, Bruce ^a  

^a Department of Obstetrics Gynecology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROLYASE; PREPHENATE DEHYDRATASE;

AMINO ACID SYNTHESIS; ARTICLE; CATALYSIS; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BINDING SITES; CALORIMETRY; CATALYSIS; CHORISMATE MUTASE; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; CONSERVED SEQUENCE; CYCLOHEXANECARBOXYLIC ACIDS; CYCLOHEXENES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FEEDBACK; FLUORESCENCE; KINETICS; MULTIENZYME COMPLEXES; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHENYLALANINE; PREPHENATE DEHYDRATASE; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS; TITRIMETRY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; FELIS CATUS;

EID: 0034712711     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9926680     Document Type: Article

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