Structural characterization of a D-isomer specific 2-hydroxyacid dehydrogenase from Lactobacillus delbrueckii ssp. bulgaricus

Journal of Structural Biology

Volumn 181, Issue 2, 2013, Pages 179-184

  Holton, Simon J ^a   Anandhakrishnan, Madhankumar ^a   Geerlof, Arie ^a,b   Wilmanns, Matthias ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b Institute of Structural Biology   (Germany)

Author keywords

Lactic acid; Lactobacillus delbrueckii ssp. bulgaricus; NAD+ dependent dehydrogenase; X ray crystallography

Indexed keywords

2 HYDROXYACID DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; RESIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CRYSTALLIZATION; DISSOCIATION CONSTANT; ENZYME ACTIVITY; ENZYME BINDING; ENZYME PURIFICATION; ENZYME STRUCTURE; HYDROGEN BOND; HYDROPHILICITY; HYDROPHOBICITY; LACTOBACILLUS BULGARICUS; MICHAELIS MENTEN KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION;

ALCOHOL OXIDOREDUCTASES; CRYSTALLOGRAPHY, X-RAY; ISOMERISM; LACTOBACILLUS DELBRUECKII; MODELS, MOLECULAR; NAD; PROTEIN BINDING; PROTEIN CONFORMATION;

LACTOBACILLUS DELBRUECKII;

EID: 84873157959     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2012.10.009     Document Type: Article

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