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2006 | 53 | 3 | 585-589
Article title

Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli

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Abstracts
EN
DsbA is the major oxidase responsible for generation of disulfide bonds in proteins of E. coli envelope. In the present work we provided the first detailed characterization of disulfide exchange between DsbA and its natural substrate, HtrA protease. We demonstrated that HtrA oxidation relies on DsbA, both in vivo and in vitro. We followed the disulfide exchange between these proteins spectrofluorimetrically and found that DsbA oxidizes HtrA with a 1 : 1 stoichiometry. The calculated second-order apparent rate constant (kapp) of this reaction was 3.3 × 104 ± 0.6 × 104 M-1s-1. This value was significantly higher than the values obtained for nonfunctional disulfide exchanges between DsbA and DsbC or DsbD and it was comparable to the kapp values calculated for in vitro oxidation of certain non-natural DsbA substrates of eukaryotic origin.
Publisher

Year
Volume
53
Issue
3
Pages
585-589
Physical description
Dates
published
2006
received
2006-03-20
revised
2006-08-30
accepted
2006-09-16
(unknown)
2006-10-01
Contributors
  • Department of Biochemistry, University of Gdańsk, Gdańsk, Poland
  • Department of Biochemistry, University of Gdańsk, Gdańsk, Poland
  • Department of Biochemistry, University of Gdańsk, Gdańsk, Poland
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv53p585kz
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