NAD(P)H oxidase v from Lactobacillus plantarum (NoxV) displays enhanced operational stability even in absence of reducing agents

Journal of Molecular Catalysis B: Enzymatic

Volumn 71, Issue 3-4, 2011, Pages 159-165

  Park, Jonathan T ^a   Hirano, Jun Ichiro ^a,d   Thangavel, Vaijayanthi ^a,e   Riebel, Bettina R ^b   Bommarius, Andreas S ^a,c  

^a Georgia Institute of Technology   (United States)

^b EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c GEORGIA INSTITUTE OF TECHNOLOGY   (United States)

^d MITSUBISHI CHEMICAL CORPORATION   (Japan)

^e KYOTO UNIVERSITY   (Japan)

Author keywords

Cofactor; Cofactor regeneration; Cofactor specificity; NADH oxidase; Overoxidation; Total turnover number

Indexed keywords

COFACTOR REGENERATION; COFACTOR SPECIFICITY; COFACTORS; NADH OXIDASE; OVEROXIDATIONS; TOTAL TURNOVER;

AMINO ACIDS; ENZYME ACTIVITY; MOLECULAR OXYGEN; SUBSTRATES; SUGARS;

REDUCING AGENTS;

DITHIOTHREITOL; OXIDOREDUCTASE; PROTEIN NOX 5; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCING AGENT; UNCLASSIFIED DRUG;

ARTICLE; CELL LYSATE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME PURIFICATION; GENE MUTATION; GENE OVEREXPRESSION; LACTOBACILLUS PLANTARUM; NONHUMAN; OXIDATION; PH; TEMPERATURE; TURNOVER TIME;

APIS; LACTOBACILLUS PLANTARUM;

EID: 79957979256     PISSN: 13811177     EISSN: 18733158     Source Type: Journal    
DOI: 10.1016/j.molcatb.2011.04.013     Document Type: Article

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