Pyranose dehydrogenase (PDH) is a monomeric, glycosylated flavoprotein of around 65 kDa containing covalently bound FAD. As fungal flavin dependent sugar oxidoreductase PDH probably fulfills similar biological functions in lignocellulose breakdown as fungal pyranose oxidase and cellobiose dehydrogenase, which are structurally and catalytically relateD. In addition to pdh1, two similar genes are found in Agaricus meleagris (pdh2, and pdh3), which all display a highly similar sequence. Because of their high similarity to the pdh1 gene from A. meleagris and the pdh gene from A. xanthoderma, pdh2 and pdh3 most likely encode enzymes with PDH activities. Previous attempts to confirm this have been unsuccessful, as no active PDH2 or PDH3 protein could be obtained in sufficient amounts. In the present study, we investigated the catalytic properties of PDH1, PDH2, and PDH3. Depending on the expression strategy, two differently colored pools of PDH3 were obtained, which were depicted PDH3y and PDH3g, due to their yellow or green color, respectively. These PDH isoforms were produced, purified and kinetically characterized. The obtained data were compared to each other to get insights about why A. meleagris produces three highly similar PDH enzymes. The results indicate predominantly a difference between the catalytic efficiencies for electron acceptors.