Roles of His205, His296, His303 and Asp259 in catalysis by NAD+- specific D-lactate dehydrogenase

European Journal of Biochemistry

Volumn 267, Issue 6, 2000, Pages 1633-1639

  Kochhar, Sunil ^a   Lamzin, Victor S ^b   Razeto, Adelia ^b   Delley, Michele ^a   Hottinger, Herbert ^a   Germond, Jacques Edouard ^a  

^a NESTLÉ RESEARCH CENTER   (Switzerland)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

D 2 hydroxy acid dehydrogenases; D lactate dehydrogenase; Lactobacillus bulgaricus; Site directed mutagenesis

Indexed keywords

ASPARTIC ACID; DEXTRO LACTATE DEHYDROGENASE; HISTIDINE; LYSINE; PYRUVIC ACID;

ARTICLE; CATALYSIS; COENZYME; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME STRUCTURE; PH; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

AMINO ACID SUBSTITUTION; ASPARTIC ACID; BACTERIAL PROTEINS; BINDING SITES; CATALYSIS; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; L-LACTATE DEHYDROGENASE; LACTATE DEHYDROGENASES; LACTOBACILLUS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NAD; POINT MUTATION; RECOMBINANT FUSION PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

FELIS CATUS; LACTOBACILLUS; LACTOBACILLUS DELBRUECKII SUBSP. BULGARICUS;

EID: 0034061203     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01155.x     Document Type: Article

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