Evolution of enzymatic activities in the enolase superfamily: Crystallographic and mutagenesis studies of the reaction catalyzed by D- glucarate dehydratase from Escherichia coli

Biochemistry

Volumn 39, Issue 16, 2000, Pages 4590-4602

  Gulick, Andrew M ^a   Hubbard, Brian K ^b   Gerlt, John A ^b   Rayment, Ivan ^a,c  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^c Department of Biochemistry ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE DERIVATIVE; ENOLASE; HYDROLYASE;

ARTICLE; ENZYME ACTIVITY; ENZYME STRUCTURE; ESCHERICHIA COLI; MOLECULAR EVOLUTION; NONHUMAN; PRIORITY JOURNAL; SEQUENCE HOMOLOGY;

AMINO ACID SUBSTITUTION; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; EVOLUTION, MOLECULAR; GLUCARIC ACID; HYDRO-LYASES; HYDROXAMIC ACIDS; KINETICS; LIGANDS; MAGNESIUM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIGENE FAMILY; MUTATION; PHOSPHOPYRUVATE HYDRATASE; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP; SUGAR ACIDS;

ESCHERICHIA COLI;

EID: 0034712668     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi992782i     Document Type: Article

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