The primary structure of iron superoxide dismutase from Escherichia coli

FEBS Letters

Puget, Krystyna¹  Barra, Donatella²  Schininà, M.Eugenia²  Bossa, Francesco²  Michelson, Adolf M.¹  Maffey, Letizia² 

[1] Fondation Edmond de Rothschild, Institut de Biologie Physico-Chimique, Paris, France;Department of Biochemical Sciences and CNR Centre for Molecular Biology, University of Rome La Sapienza, 00185 Rome, Italy

关键词: Iron superoxide dismutase;    Primary structure;    Sequence homology;   

DOI  :  10.1016/0014-5793(87)80357-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The complete amino acid sequence of iron superoxide from Escherichia coli has been determined. The sequence was deduced from analysis of peptides obtained after cleavage of the carboxymethylated apoenzyme with trypsin, Stapholococcus aureus protease or CNBr. The polypeptide chain is made up of 192 residues and is easily aligned with the other known amino acid sequences of iron and manganese superoxide dismutases from various sources. The iron superoxide dismutase from E. coli shows a significantly higher homology with the iron enzyme from a different organism than with the manganese isoenzyme from E. coli.

【 授权许可】

Unknown