Molecular and catalytic properties of a peroxiredoxin–glutaredoxin hybrid from Neisseria meningitidis

FEBS Letters

Jacquot, Jean-Pierre¹  Rouhier, Nicolas¹ 

[1] UMR 1136 Interactions Arbres Microorganismes INRA UHP, Faculté des Sciences, P.O. Box 239, 54506 Vandoeuvre Cedex, France

关键词: Glutaredoxin;    Glutathione;    Hydroperoxide;    Peroxiredoxin;    Neisseria;    DHA;    dehydroascorbate;    DTT;    dithiothreitol;    Grx;    glutaredoxin;    GR;    glutathione reductase;    GSH;    reduced glutathione;    Prx;    peroxiredoxin;    Trx;    thioredoxin;   

DOI  :  10.1016/S0014-5793(03)01156-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A hybrid protein from Neisseria meningitidis, which contains both a peroxiredoxin and a glutaredoxin domain, has been isolated. The enzyme was active in the reduction of various peroxides and dehydroascorbate in the presence of reduced glutathione. These findings suggest that both the peroxiredoxin and glutaredoxin domains are biochemically active in the fusion. Moreover, when expressed separately, the glutaredoxin domain was catalytically active and the peroxiredoxin domain possessed a weak activity when supplemented with exogenous glutaredoxin.

【 授权许可】

Unknown