Evolution of enzymatic activities in the enolase superfamily: D-tartrate dehydratase from Bradyrhizobium japonicum

Biochemistry

Volumn 45, Issue 49, 2006, Pages 14598-14608

  Yew, Wen Shan ^a   Fedorov, Alexander A ^b   Fedorov, Elena V ^b   Wood, Bryant McKay ^a   Almo, Steven C ^b   Gerlt, John A ^a  

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

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; DECOMPOSITION; DEHYDRATION; GENETIC ENGINEERING; MICROORGANISMS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; REACTION KINETICS;

DEHYDRATASE; ENEDIOLATE INTERMEDIATES; LIGANDS; OXALOACETATE;

ENZYME IMMOBILIZATION;

ACID; ACID SUGAR; ASPARTIC ACID; BASE; CARBOHYDRATE; DEXTRO TARTRATE; DEXTRO TARTRATE DEHYDRATASE; ENEDIOLATE; ENOLASE; ESTER; FUNCTIONAL GROUP; GLUTAMIC ACID; HYDROGEN; HYDROLYASE; HYDROXYL GROUP; LYSINE; MAGNESIUM ION; MANDELATE RACEMASE; MUTANT PROTEIN; OXALOACETIC ACID; SOLVENT; WATER;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENOME; BETA SHEET; BRADYRHIZOBIUM JAPONICUM; CATALYSIS; CATALYST; CONTROLLED STUDY; DECOMPOSITION; ELIMINATION REACTION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; EVOLUTION; HYDRATION; KINETICS; MOLECULAR STABILITY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FUNCTION; PROTON NUCLEAR MAGNETIC RESONANCE; PROTON TRANSPORT; STEREOCHEMISTRY; STRUCTURE ACTIVITY RELATION;

BACTERIAL PROTEINS; BASE SEQUENCE; BINDING SITES; BRADYRHIZOBIUM; DNA PRIMERS; EVOLUTION, MOLECULAR; HYDRO-LYASES; KINETICS; MAGNESIUM; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; NAD; PHOSPHOPYRUVATE HYDRATASE; PROTEIN CONFORMATION;

BRADYRHIZOBIUM JAPONICUM;

EID: 33845398832     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061688g     Document Type: Article

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