Fungal riboflavin 5'-hydroxymethyl dehydrogenase catalyzes formation of both the aldehyde (riboflavinal) and the acid (riboflavinoic acid).
The purified enzyme from Schizophyllum commune that readily catalyzes the oxidation of the 5'-hydroxymethyl function of riboflavin (vitamin B2) with a redox dye and O2 to form the 5'-aldehyde can more slowly further oxidize the 5'-aldehyde to the 5'-acid. Hence, the formation of these so-called 'schizoflavins' can be accounted for by the action of one enzyme.
Chen
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Department of Biochemistry, Rollins Research Center, Emory University, Atlanta, GA 30322-3050, USA.
McCormick
D B
DB
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D002384:Catalysis; D005415:Flavins / Q000378:metabolism*; D012256:Riboflavin / Q000031:analogs & derivatives* / Q000378:metabolism*; D012567:Schizophyllum / Q000201:enzymology*; D013379:Substrate Specificity
D005415:Flavins; C024382:schizoflavins; C023849:vitamin B2 aldehyde; D000429:Alcohol Oxidoreductases; C029140:vitamin B2-aldehyde-forming enzyme; D012256:Riboflavin