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The specificity of horse liver alcohol dehydrogenase for cyclohexanol and its 3-methyl derivatives was investigated by stopped-flow and initial velocity kinetic studies. The (1S,3S)-3-methylcyclohexanol was 7 times more reactive (V/Km) than cyclohexanol, whereas the (1R,3R)-3-methylcyclohexanol was at least 1000 times less reactive than its enantiomer. Computer simulation of the transient reaction of NAD+ and the cyclohexanols catalyzed by the enzyme suggests that the rate of transfer of hydrogen from the alcohol to NAD+ is increased with the 1S,3S isomer. Modeling of the three-dimensional structure of the ternary complex of the enzyme suggests that the 1S,3S isomer should only bind in a productive, reactive mode, whereas the 1R,3R isomer would bind predominantly in a nonproductive, inhibitory mode.
K M Lee, and
K F Dahlhauser, and
B V Plapp
June 1966,
Journal of molecular biology,
K M Lee, and
K F Dahlhauser, and
B V Plapp
June 1965,
Biochemistry,
K M Lee, and
K F Dahlhauser, and
B V Plapp
September 1974,
Biochemical and biophysical research communications,
K M Lee, and
K F Dahlhauser, and
B V Plapp
March 1972,
Biochemical and biophysical research communications,
K M Lee, and
K F Dahlhauser, and
B V Plapp
August 1948,
Archives of biochemistry,
K M Lee, and
K F Dahlhauser, and
B V Plapp
August 1974,
FEBS letters,
K M Lee, and
K F Dahlhauser, and
B V Plapp
January 1984,
Journal of applied biochemistry,
K M Lee, and
K F Dahlhauser, and
B V Plapp
April 1969,
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K M Lee, and
K F Dahlhauser, and
B V Plapp
November 1975,
European journal of biochemistry,
K M Lee, and
K F Dahlhauser, and
B V Plapp
February 1972,
Enzymologia,
