Complex formation of apo-enzyme, coenzyme and substrate of d-amino acid oxidase IV. Changes in physico-chemical properties of the protein

Abstract

1. 1. A molecular weight of 115 000 was found for the apo- d-amino acid oxidase, for the holo- d-amino acid oxidase and for the artificial Michaelis complex of this enzyme with benzoate. 2. 2. The differences in s 20 ,w, D 20 ,w, v, [η] and [α] D 20 of these three products all point to configurations of the protein part, viz. an increase of α-helix and decrease of random coiling in the order apo-enzyme, holo-enzyme, artificial Michaelis complex. 3. 3. It is suggested that these changes are also involved in the action of d-amino acid oxidase.