Evolution of enzymatic activities in the enolase superfamily: Structure of a substrate-liganded complex of the L-Ala-D/L-Glu epimerase from Bacillus subtilis

Biochemistry

Volumn 43, Issue 32, 2004, Pages 10370-10378

  Klenchin, Vadim A ^a   Schmidt, Dawn M ^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

BACTERIA; CATALYSIS; ENZYME KINETICS; GENES; HYDROGEN BONDS; POLYPEPTIDES;

ENZYMATIC ACTIVITIES; PROTON TRANSFER REACTION;

BIOCHEMISTRY;

ENOLASE; EPIMERASE;

ARTICLE; BACILLUS SUBTILIS; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; STEREOCHEMISTRY; STRUCTURE ACTIVITY RELATION;

AMINO ACID ISOMERASES; BACILLUS SUBTILIS; CRYSTALLOGRAPHY, X-RAY; EVOLUTION, MOLECULAR; LIGANDS; PHOSPHOPYRUVATE HYDRATASE; PROTEIN BINDING; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); POSIBACTERIA;

EID: 4043106218     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049197o     Document Type: Article

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