The functional properties of DsbG, a thiol‐disulfide oxidoreductase from the periplasm of Escherichia coli

FEBS Letters

Raina, Satish²  Missiakas, Dominique³  van Straaten, Monique¹  Darby, Nigel J.¹ 

[1] The European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69012 Heidelberg, Germany;Département de Biochimie Médicale, Centre Médical Universitaire, 1 Rue Michel-Servet, 1211 Geneva 4, Switzerland;CNRS UPR 9027, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France

关键词: Disulfide bond;    Protein folding;    Dsb protein;    Thioredoxin;    BPTI;    bovine pancreatic trypsin inhibitor;    DsbGS S and DsbGSH SH;    the disulfide and dithiol forms of protein DsbG;    respectively;    DTT;    dithiothreitol;    PSH SH;    peptide substrate containing cysteine residues at positions 2 and 27;    GSSG and GSH;    the oxidized and reduced forms of glutathione;    respectively;    HPLC;    high pressure liquid chromatography;    PDI;    protein disulfide isomerase;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/S0014-5793(98)00539-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Genetic studies have recently identified DsbG, a new member of the dsb group of redox proteins, which catalyze protein disulfide bond formation in the periplasm of Escherichia coli. We now demonstrate that DsbG functions primarily as an oxidant during protein disulfide bond formation, which is consistent with the low stability of its active site disulfide bond. There are indications, however, that the substrate range of DsbG may be narrower than the other periplasmic oxidative enzymes, DsbA and DsbC. Our observations further elaborate the pathway of disulfide bond formation in E. coli.

【 授权许可】

Unknown