The amino acid sequence of D-amino acid oxidase from Rhodotorula gracilis was determined by automated Edman degradation of peptides generated by enzymatic 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 peroxisomal targeting. Moreover, Rhodotorula gracilis D-amino acid oxidase contains a region with a cluster of basic amino acids, probably exposed to solvent, which is absent in other D-amino acid oxidases.
The primary structure of D-amino acid oxidase from Rhodotorula gracilis / L. Faotto, L. Pollegioni, F. Ceciliani, S. Ronchi, M.S. Pilone. - In: BIOTECHNOLOGY LETTERS. - ISSN 0141-5492. - 17:2(1995 Feb), pp. 193-198. [10.1007/BF00127987]
The primary structure of D-amino acid oxidase from Rhodotorula gracilis
F. Ceciliani;S. RonchiPenultimo
;
1995
Abstract
The amino acid sequence of D-amino acid oxidase from Rhodotorula gracilis was determined by automated Edman degradation of peptides generated by enzymatic 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 peroxisomal targeting. Moreover, Rhodotorula gracilis D-amino acid oxidase contains a region with a cluster of basic amino acids, probably exposed to solvent, which is absent in other D-amino acid oxidases.
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