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The novel enzyme of Schizophyllum commune which converts the 5•L hydroxymethyl group of riboflavin to the aldehyde group has been found to be unable to use NAD(P)+, FMN, FAD and Cyt c as electron acceptor for the conversion, as reported previously (1 , 2). During further investigation on the reaction mechanism of the enzyme , we have found a significant inhibition of the enzyme by ƒ¿-tocopherol, as detailed in this paper . The enzyme was purified about 100-fold from a cell-free extract of S . commune IFO No. 4928 by means of ammonium sulfate fractionation , ethanol fractionation, Sephadex G-25 column chromatography , and DEAE-Sephacel column chromatog raphy and the activity of the enzyme was assayed in terms of the fluorescence intensity of B2-aldehyde produced by the method described in the previous

Inhibitory effect of vitamin E on vitamin B2-aldehyde-forming enzyme in Schizophyllum commune.