Abstract:
:Protein deglutathionylation is mainly catalyzed by glutaredoxins (GRXs). We have analyzed the biochemical properties of four of the six different GRXs of Chlamydomonas reinhardtii. Kinetic parameters were determined for disulfide and dehydroascorbate reduction but also for deglutathionylation of artificial and protein substrates. The results indicate that GRXs exhibit striking differences in their catalytic properties, mainly linked to the class of GRX considered but also to the pK(a) of the N-terminal catalytic cysteine. Furthermore, glutathionylated proteins were found to exhibit distinct reactivities with GRXs. These results suggest that glutathionylation may allow a fine tuning of cell metabolism under stress conditions.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Gao XH,Zaffagnini M,Bedhomme M,Michelet L,Cassier-Chauvat C,Decottignies P,Lemaire SDdoi
10.1016/j.febslet.2010.04.034subject
Has Abstractpub_date
2010-06-03 00:00:00pages
2242-8issue
11eissn
0014-5793issn
1873-3468pii
S0014-5793(10)00304-2journal_volume
584pub_type
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