Mutations in adenine-binding pockets enhance catalytic properties of NAD(P)H-dependent enzymes

Protein Engineering, Design and Selection

Volumn 29, Issue 1, 2015, Pages 31-38

  Cahn, J K B ^a   Baumschlager, A ^a   Brinkmann Chen, S ^a   Arnold, F H ^a  

^a California Institute of Technology   (United States)

Author keywords

directed evolution; enzyme optimality; nicotinamide cofactors; protein engineering; site saturation mutagenesis

Indexed keywords

BINS; ENZYMES; ESCHERICHIA COLI; MUTAGENESIS;

COFACTORS; DIRECTED EVOLUTION; OPTIMALITY; PROTEIN ENGINEERING; SATURATION MUTAGENESIS;

BIOCHEMICAL ENGINEERING;

ADENINE; ALCOHOL DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; PROTEIN BINDING;

ARTICLE; CATALYST; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DROSOPHILA MELANOGASTER; ENZYME ENGINEERING; ESCHERICHIA COLI; GENE MUTATION; KLEBSIELLA PNEUMONIAE; LACTOBACILLUS; LACTOBACILLUS SANFRANCISCENSIS; LACTOCOCCUS LACTIS; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; TALAROMYCES; THERMOSTABILITY; BINDING SITE; CHEMISTRY; GENETICS; METABOLISM; PROCEDURES; SITE DIRECTED MUTAGENESIS;

ADENINE; BINDING SITES; ESCHERICHIA COLI; MUTAGENESIS, SITE-DIRECTED; NADH, NADPH OXIDOREDUCTASES; NADP; PROTEIN BINDING;

EID: 84959873293     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzv057     Document Type: Article

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