DsbA is a periplasmic thiol:disulfide oxidoreductase found in Gram-negative bacteria that promotes protein disulfide bond formation. DsbA contains a redox active disulfide bond that is catalytically transferred via disulfide exchange to a diverse range of newly translocated protein substrates. The protein is restored to the oxidized state by EC 1.8.5.9, protein dithiol:quinone oxidoreductase DsbB.
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The enzyme appears in viruses and cellular organisms
disulfide oxidoreductase, DsbA, protein dithiol oxidoreductase, SdbA, Streptococcus disulfide bond protein A, TDOR, thiol-disulfide oxidoreductase, more
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a [DsbA protein] carrying a disulfide bond + a [protein] with reduced L-cysteine residues = a [DsbA protein] with reduced L-cysteine residues + a [protein] carrying a disulfide bond
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SYSTEMATIC NAME
IUBMB Comments
protein dithiol:[DsbA protein] oxidoreductase (protein disulfide-forming)
DsbA is a periplasmic thiol:disulfide oxidoreductase found in Gram-negative bacteria that promotes protein disulfide bond formation. DsbA contains a redox active disulfide bond that is catalytically transferred via disulfide exchange to a diverse range of newly translocated protein substrates. The protein is restored to the oxidized state by EC 1.8.5.9, protein dithiol:quinone oxidoreductase DsbB.
autolysin AtlS requires the enzyme for the formation of an intramolecular disulfide bond between residues Cys1048 and Cys1069. This bond is essential for processing and enzymatic activity
autolysin AtlS requires the enzyme for the formation of an intramolecular disulfide bond between residues Cys1048 and Cys1069. This bond is essential for processing and enzymatic activity
the DsbB protein rapidly reoxidizes the enzyme. The reaction strongly depends on the presence of oxygen, implying that oxygen serves as the final electron acceptor for this disulfide bond formation reaction. The enzyme acts as a high affinity substrate for DsbB with a Km of 0.096 mM and a turnover number of 0.4 s-1
autolysin AtlS requires the enzyme for the formation of an intramolecular disulfide bond between residues Cys1048 and Cys1069. This bond is essential for processing and enzymatic activity
autolysin AtlS requires the enzyme for the formation of an intramolecular disulfide bond between residues Cys1048 and Cys1069. This bond is essential for processing and enzymatic activity
the enzyme is required for protein disulfide bond formation in vivo. Disulfide-bonded enzyme is a potent oxidant and ideally suited for generating protein disulfide bonds
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the reduced enzyme form is crystallized by the dialysis method using 0.2 M ammonium acetate, 0.1 M sodium citrate pH 5.6, 30% (w/v) polyethylene glycol 4 K and 40 mM dithiothreitol. The oxidized enzyme form is crystallized by the hanging drop vapor diffusion method using 25% (w/v) polyethylene glycol 8 K in 0.1 M cacodylate buffer pH 6.5
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History
1.8.4.15 protein dithiol oxidoreductase (disulfide-forming)
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