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Title
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5-Methylnicotinamide-adenine dinucleotide. Kinetic investigation with major and minor isoenzymes of liver alcohol dehydrogenase and structural determination of its binary complex with alcohol dehydrogenase.
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Authors
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J.P.Samama,
A.D.Wrixon,
J.F.Biellmann.
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Ref.
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Eur J Biochem, 1981,
118,
479-486.
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PubMed id
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Abstract
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5-Methylnicotinamide-adenine dinucleotide and 3-cyano-5-methylpyridine-adenine
dinucleotide was prepared from 5-methylthionicotinamide-adenine dinucleotide by
chemical conversion. The 5-methylthionicotinamide-adenine dinucleotide was
obtained by enzymic transglucosidation. Model compounds ascertained the
structure. None of the dinucleotides methylated at C-5 was active with the major
isoenzyme EE of horse liver alcohol dehydrogenase, but activity with
5-methylnicotinamide-adenine dinucleotide was measured with the minor
isoenzymes. The binding of 5-methylnicotinamide-adenine dinucleotide to liver
alcohol dehydrogenase, investigated by X-ray diffraction methods to 0.37-nm
resolution, occurs with the pyridinium ring away from the active site as
previously described for 3-iodopyridine-adenine and pyridine-adenine
dinucleotides. A general conclusion on the use of inhibitors as tools for
exploration of the active site is drawn.
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