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- W2163473419 endingPage "1960" @default.
- W2163473419 startingPage "1954" @default.
- W2163473419 abstract "ABSTRACT The quinohemoprotein tetrahydrofurfuryl alcohol dehydrogenase (THFA-DH) from Ralstonia eutropha strain Bo was investigated for its catalytic properties. The apparent k cat / K m and K i values for several substrates were determined using ferricyanide as an artificial electron acceptor. The highest catalytic efficiency was obtained with n -pentanol exhibiting a k cat / K m value of 788 × 10 4 M −1 s −1 . The enzyme showed substrate inhibition kinetics for most of the alcohols and aldehydes investigated. A stereoselective oxidation of chiral alcohols with a varying enantiomeric preference was observed. Initial rate studies using ethanol and acetaldehyde as substrates revealed that a ping-pong mechanism can be assumed for in vitro catalysis of THFA-DH. The gene encoding THFA-DH from R. eutropha strain Bo ( tfaA ) has been cloned and sequenced. The derived amino acid sequence showed an identity of up to 67% to the sequence of various quinoprotein and quinohemoprotein dehydrogenases. A comparison of the deduced sequence with the N-terminal amino acid sequence previously determined by Edman degradation analysis suggested the presence of a signal sequence of 27 residues. The primary structure of TfaA indicated that the protein has a tertiary structure quite similar to those of other quinoprotein dehydrogenases." @default.
- W2163473419 created "2016-06-24" @default.
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- W2163473419 creator A5010552265 @default.
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- W2163473419 date "2001-03-15" @default.
- W2163473419 modified "2023-10-18" @default.
- W2163473419 title "Catalytic and Molecular Properties of the Quinohemoprotein Tetrahydrofurfuryl Alcohol Dehydrogenase from Ralstonia eutropha Strain Bo" @default.
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- W2163473419 doi "https://doi.org/10.1128/jb.183.6.1954-1960.2001" @default.
- W2163473419 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/95090" @default.
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