Molecular and catalytic properties of a peroxiredoxin-glutaredoxin hybrid from Neisseria meningitidis.
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.
UMR 1136 Interactions Arbres Microorganismes INRA UHP, Faculté des Sciences, P.O. Box 239, 54506 Vandoeuvre, France. nrouhier@scbiol.uhp-nancy.fr
Nicolas
N
Rouhier
Jean Pierre
JP
Jacquot
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics; D002384:Catalysis; D003683:Dehydroascorbic Acid / Q000378:metabolism; D054477:Glutaredoxins; D009345:Neisseria meningitidis / Q000737:chemistry*; D010088:Oxidoreductases; D010544:Peroxidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010545:Peroxides / Q000378:metabolism; D054464:Peroxiredoxins; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D054477:Glutaredoxins; D010545:Peroxides; D011506:Proteins; D011993:Recombinant Fusion Proteins; D010088:Oxidoreductases; D010544:Peroxidases; D054464:Peroxiredoxins; D003683:Dehydroascorbic Acid