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3-Ketovalidoxylamine A C-N lyase was purified about 900-fold from the cell-free extract of Flavobacterium saccharophilum by ammonium sulfate fractionation, column chromatography on CM cellulose and gel filtration on Sephacryl S-200. The purified enzyme was homogeneous as judged by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The molecular weight of the enzyme was estimated to be 36,000 by gel filtration on Sephacryl S-200 and by SDS polyacrylamide gel electrophoresis, indicating that the enzyme is a monomer. The optimum pH was found at 9.0. The enzyme activity was inhibited by EDTA or ethyleneglycol bis(beta-aminoethylether)-N,N'-tetraacetic acid and the inhibition was reversed by Ca2+ ion. The enzyme was able to eliminate p-nitroaniline or p-nitrophenol from p-nitrophenyl-3-ketovalidamine (IV) or p-nitrophenyl-alpha-D-3-ketoglucoside (VI), but not from p-nitrophenyl-1-epi-3-ketovalidamine or p-nitrophenyl-beta-D-3-ketoglucoside. Apparent Km values for IV and VI were 0.24 mM and 0.5 mM, respectively.
M Takeuchi, and
N Asano, and
Y Kameda, and
K Matsui
October 2010,
Applied biochemistry and biotechnology,
M Takeuchi, and
N Asano, and
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K Matsui
January 2007,
Applied microbiology and biotechnology,
M Takeuchi, and
N Asano, and
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K Matsui
May 1990,
Chemical & pharmaceutical bulletin,
M Takeuchi, and
N Asano, and
Y Kameda, and
K Matsui
August 1984,
Journal of biochemistry,
M Takeuchi, and
N Asano, and
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K Matsui
June 1970,
Biochimica et biophysica acta,
M Takeuchi, and
N Asano, and
Y Kameda, and
K Matsui
September 1981,
The Journal of antibiotics,
M Takeuchi, and
N Asano, and
Y Kameda, and
K Matsui
December 1980,
The Journal of antibiotics,
M Takeuchi, and
N Asano, and
Y Kameda, and
K Matsui
February 1975,
Biochimica et biophysica acta,
M Takeuchi, and
N Asano, and
Y Kameda, and
K Matsui
September 1988,
Journal of biochemistry,
M Takeuchi, and
N Asano, and
Y Kameda, and
K Matsui
May 1980,
The Journal of biological chemistry,
