Directed evolution of a formate dehydrogenase for increased tolerance to ionic liquids reveals a new site for increasing the stability

ChemBioChem

Volumn 15, Issue 18, 2014, Pages 2710-2718

  Carter, Julie L L ^a   Bekhouche, Mourad ^a   Noiriel, Alexandre ^a   Blum, Loïc J ^a   Doumèche, Bastien ^a  

^a UNIVERSITÉ LYON 1   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME VARIANT; FORMATE DEHYDROGENASE; FORMAZAN; GLUTAMIC ACID; IONIC LIQUID; MONOMER; MUTANT PROTEIN; PHOSPHATE; 1,3-DIMETHYLIMIDAZOLIUM; IMIDAZOLE DERIVATIVE;

AQUEOUS SOLUTION; ARTICLE; BIOCATALYSIS; CANDIDA BOIDINII; CONTROLLED STUDY; DIRECTED MOLECULAR EVOLUTION; ENZYME KINETICS; ENZYME STABILITY; FLUORESCENCE ANALYSIS; GENETIC SCREENING; MOLECULAR MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; PKA; POLYMERASE CHAIN REACTION; SITE DIRECTED MUTAGENESIS; STEADY STATE; WILD TYPE; CANDIDA; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; MUTATION; PROTEIN UNFOLDING;

CANDIDA; DIRECTED MOLECULAR EVOLUTION; ENZYME STABILITY; FORMATE DEHYDROGENASES; IMIDAZOLES; IONIC LIQUIDS; MODELS, MOLECULAR; MUTATION; PROTEIN UNFOLDING;

EID: 84915809570     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.201402501     Document Type: Article

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