Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus

Journal of Molecular Biology

Volumn 318, Issue 1, 2002, Pages 109-119

  Razeto, Adelia ^a   Kochhar, Sunil ^b   Hottinger, Herbert ^b   Dauter, Miroslava ^a   Wilson, Keith S ^c   Lamzin, Victor S ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b NESTLÉ RESEARCH CENTER   (Switzerland)

^c UNIVERSITY OF YORK   (United Kingdom)

Author keywords

Conformational asymmetry; D lactate dehydrogenase; Domain closure; Stereoselectivity; Substrate specificity

Indexed keywords

DEXTRO LACTATE DEHYDROGENASE; PYRUVIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SULFATE;

ARTICLE; BINDING SITE; CATALYSIS; CATALYST; CHEMICAL STRUCTURE; COENZYME; CONTROLLED STUDY; CRYSTAL; ENZYME ACTIVATION; ENZYME SPECIFICITY; HYDROPHOBICITY; KINETICS; LACTOBACILLUS; LACTOBACILLUS BULGARIS; LACTOBACILLUS HELVETICUS; MOLECULAR BIOLOGY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTON TRANSPORT; REDUCTION; X RAY ANALYSIS;

LACTOBACILLUS; LACTOBACILLUS DELBRUECKII SUBSP. BULGARICUS; LACTOBACILLUS HELVETICUS;

EID: 0036307726     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00086-4     Document Type: Article

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