The crystal structure of R-specific alcohol dehydrogenase from Lactobacillus brevis suggests the structural basis of its metal dependency

Journal of Molecular Biology

Volumn 327, Issue 2, 2003, Pages 317-328

  Niefind, Karsten ^a   Müller, Jörg ^a,c   Riebel, Bettina ^b,d   Hummel, Werner ^b   Schomburg, Dietmar ^a  

^a UNIVERSITY OF COLOGNE   (Germany)

^b FORSCHUNGSZENTRUM JÜLICH   (Germany)

^c SANOFI   (France)

^d EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Lactobacillus brevis; Mg2+ dependency; R alcohol dehydrogenase; Short chain dehydrogenase reductase (SDR); X ray crystallography

Indexed keywords

ACETOPHENONE; ALCOHOL DEHYDROGENASE; AMINO ACID; BACTERIAL ENZYME; EDETIC ACID; MAGNESIUM ION; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TETRAMER;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENANTIOSELECTIVITY; ENZYME ACTIVE SITE; ENZYME INACTIVATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; LACTOBACILLUS BREVIS; METAL BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

LACTOBACILLUS; LACTOBACILLUS BREVIS;

EID: 0037459232     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00081-0     Document Type: Article

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