The primary structure of superoxide dismutase purified from anaerobically maintained Bacteroides gingivalis

FEBS Letters

Amano, Atsuo²  Tsunemitsu, Akira²  Tsunasawa, Susumu¹  Shizukuishi, Satoshi²  Maekawa, Kazuhiko¹ 

[1] Division of Protein Chemistry, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565, Japan;Department of Preventive Dentistry, Faculty of Dentistry, Osaka University, 1-8 Yamadaoka, Suita, Osaka 565, Japan

关键词: Amino acid sequence;    Superoxide dismutase;    Bacteroides gingivalis;   

DOI  :  10.1016/0014-5793(90)80488-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The superoxide dismutase (SOD) of Bacteroides gingivalis can use either iron or manganese as a cofactor in its catalytic activity. In this study, the complete amino acid sequence of this SOD purified from anaerobically maintained B. gingivalis cells was determined. The proteins consisted of 191 amino acid residues and had a molecular mass of 21 500. The sequence of B. gingivalis SOD showed 44–51% homology with those for iron-specific SODs (Fe-SODs) and 40–45% homology with manganese-specific SODs (Mn-SODs) from several bacteria. However, this sequence homology was considerably less than that seen among the Fe-SOD (65–74%) or Mn-SOD family (42–60%). This indicates that B. gingivalis SOD, which accepts either iron or manganese as metal cofactor, is a structural intermediate between the Fe-SOD and Mn-SOD families.

【 授权许可】

Unknown