The primary structure of D-amino acid oxidase fromRhodotorula gracilis

✍ Scribed by Ludovica Faotto; Loredano Pollegioni; Fabrizio Ceciliani; Severino Ronchi; Mirella S. Pilone

• Book ID: 104632822
• Publisher: Springer Netherlands
• Year: 1995
• Tongue: English
• Weight: 436 KB
• Volume: 17
• Category: Article
• ISSN: 0141-5492
• DOI: 10.1007/bf00127987

✦ Synopsis

The amino acid sequence of D-amino acid oxidase from Rhodotoruta gracitis was determined by automated Edman degradation of peptides generated by enz3matic and chemical cleavage. The enzyme monomer contains 368 amino acid residues and its sequence is homologous to that of other known D-amino acid oxidases. Six highly conserved regions appear to have a specific role in binding of coenzyme FAD, in active site topology and in pero,-dsomal targeting. Moreover, Rhodotorula gracilis D-amino acid o~dase contains a region with a cluster of basic amino acids, probably exposed to solvent, which is absent in other D-amino acid oxidases.