A single-point mutation enables lactate dehydrogenase from Bacillus subtilis to utilize NAD+ and NADP+ as cofactor

Engineering in Life Sciences

Volumn 11, Issue 1, 2011, Pages 26-36

  Richter, Nina ^a   Zienert, Anke ^b   Hummel, Werner ^b  

^a Evocatal GmbH   (Germany)

^b HEINRICH HEINE UNIVERSITY   (Germany)

Author keywords

Bacillus subtilis; Cofactor specificity; Lactate dehydrogenase; Saturation mutagenesis; Structure guided mutagenesis

Indexed keywords

BACILLUS SUBTILIS; COFACTOR SPECIFICITY; LACTATE DEHYDROGENASE; SATURATION MUTAGENESIS; STRUCTURE-GUIDED MUTAGENESIS;

AMINO ACIDS; BACILLI; BACTERIOLOGY; ENZYMES; MUTAGENESIS;

ORGANIC POLYMERS;

AMINO ACID; LACTATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

AMINO ACID; BACTERIUM; BIOCHEMISTRY; CATALYSIS; ENZYME ACTIVITY; MUTATION; PROTEIN; REACTION KINETICS; REDUCTION;

ARTICLE; BACILLUS SUBTILIS; CATALYSIS; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; MUTAGENESIS; NONHUMAN; PH MEASUREMENT; POINT MUTATION; PROTEIN EXPRESSION; SITE SATURATION MUTAGENESIS; TEMPERATURE MEASUREMENT;

BACILLUS SUBTILIS; LACTOBACILLUS KEFIRI;

EID: 79951646335     PISSN: 16180240     EISSN: 16182863     Source Type: Journal    
DOI: 10.1002/elsc.201000151     Document Type: Article

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