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A new enzyme, fructosyl-amino acid oxidase (fructosyl-α-l-amino acid: oxygen oxidoreductase (defructosylating)) was found, which decomposes Amadori rearrangement compounds of α-l-amino acids to the corresponding α-ketoaldehydes and α-l-amino acids. The enzyme was purified from a strain of Corynebacterium sp. about 38.9-fold to a single protein band with an overall yield of 35 % from the crude extract, and crystallized in rhombic plates. The molecular weight of the enzyme was about 88,000 on gel filtration and 44,000 on SDS-polyacrylamide gel electrophoresis. Non-covalently bound FAD was the prosthetic group. Its isoelectric point was pH 4.6. The optimum pH of the enzyme reaction in potassium phosphate buffer was about 8.3. Fructosyl-α-l-amino acid was the substrate having the highest susceptibility to the enzyme, but N-fructosyl derivatives of other materials, such as β-amino acids, l-imino acids, d-amino acids, alkyl amines, and ammonia, showed almost no susceptibility. The apparent Km values for fructos...

Purification and properties of fructosyl-amino acid oxidase from Corynebacterium sp. 2-4-1.