THE PRIMARY STRUCTURE OF D-AMINO-ACID OXIDASE FROM RHODOTORULA-GRACILIS

The amino acid sequence of D-amino acid o;xidase from Rhodotorula grac ilis was determined by automated Edman degradation of peptides generat ed by enzymatic and chemical cleavage. The enzyme monomer contains 368 amino acid residues and its sequence is homologous to that of other k nown D-amino acid oxidases. Six highly conserved regions appear to hav e a specific role in binding of coenzyme FAD, in active site topology and in peroxisomal targeting. Moreover, Rhodotorula gracilis D-amino a cid oxidase contains a region with a cluster of basic amino acids, pro bably exposed to solvent, which is absent in other D-amino acid oxidas es.