Abstract:
:We have examined the activity of protein disulfide isomerase (PDI) and glutaredoxin (Grx) 1, 2 and 3 from Escherichia coli to catalyze the cleavage of glutathionylated ribonuclease A (RNase-SG) by 1 mM GSH to yield reduced RNase. Apparent Km values for RNase-SG were similar, 2-10 microM, for Grx 1, 3 and PDI but Grx I and Grx 3 showed 500-fold higher turnover numbers than PDI. The atypical Grx 2 also catalyzed deglutathionylation by GSH, but had higher Km and apparent turnover number values compared to the two classical Grx. Refolding of RNase in a glutathione redox buffer was catalyzed by PDI. However, it could be measured only after a characteristic lag phase that was shortened by all three E. coli Grxs in a concentration-dependent manner. A role of the glutaredoxin mechanism in the endoplasmic reticulum is suggested.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Lundström-Ljung J,Vlamis-Gardikas A,Aslund F,Holmgren Adoi
10.1016/s0014-5793(98)01698-6subject
Has Abstractpub_date
1999-01-25 00:00:00pages
85-8issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(98)01698-6journal_volume
443pub_type
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