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

被引：50

作者：

FAOTTO, L

POLLEGIONI, L

CECILIANI, F

RONCHI, S

PILONE, MS

机构：

[1] UNIV MILAN,IST FISIOL VET & BIOCHIM,I-20122 MILAN,ITALY

[2] UNIV MILAN,DIPARTIMENTO FISIOL & BIOCHIM GEN,I-20122 MILAN,ITALY

[3] CTR INTERUNIV STUDIO MACROMOLEC INFORMAZ,I-20133 MILAN,ITALY

来源：

BIOTECHNOLOGY LETTERS | 1995年 / 17卷 / 02期

关键词：

D O I：

10.1007/BF00127987

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The amino acid sequence of D-amino acid o;xidase 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.

引用

页码：193 / 198

页数：6

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