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

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Rouhier N,Jacquot JP

doi

10.1016/s0014-5793(03)01156-6

keywords:

subject

Has Abstract

pub_date

2003-11-06 00:00:00

pages

149-53

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014579303011566

journal_volume

554

pub_type

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