Structure and Function of D-Amino Acid Oxidase

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Abstract
D-Amino acid oxidase [D-amino acid: O2 oxidoreductase (deaminating), EC 1.4.3.3] holoenzyme migrated as a single band in zone electrophoresis on an agarose plate at several pH values from 5.5 to 9.5. The isoelectric point was found at pH 6.24. In disc electrophoresis in polyacrylamide gel, the holoenzyme migrated also as a single band at pH 8.9, but separated into two bands at pH 8.2, both of which showed the enzymatic activity without the addition of the coenzyme, FAD. In the experiments of isoelectric focusing, two bands were detected in both the holoenzyme and the apoenzyme. Ultracentrifugal analysis indicated the occurrence of monomer and dimer of the holoenzyme. It was also indicated that the monomer-dimer equilibrium shifted towards monomer formation by the lowering of pH, temperature, or both of the solution and towards dimer formation as the holoenzyme was mixed with benzoate, a substrate-substitute.

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