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Literature summary extracted from

  • Ireland, P.; McMahon, R.; Marshall, L.; Halili, M.; Furlong, E.; Tay, S.; Martin, J.; Sarkar-Tyson, M.
    Disarming Burkholderia pseudomallei Structural and functional characterization of a disulfide oxidoreductase (DsbA) required for virulence in vivo (2014), Antioxid. Redox Signal., 20, 606-617 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.8.4.15 oxidized glutathione required for activity Burkholderia pseudomallei

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.4.15 expressed in Escherichia coli BL21(DE3) cells Burkholderia pseudomallei

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.15 Burkholderia pseudomallei
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.4.15 immobilized metal affinity chromatography Burkholderia pseudomallei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.15 7-amido-4-methylcoumarin-labelled cysteine pair-containing reporter peptide substrate + oxidized europium
-
 Burkholderia pseudomallei ?
-
 ?
1.8.4.15 insulin + dithiothreitol
-
 Burkholderia pseudomallei ?
-
 ?
1.8.4.15 additional information in the absence of oxidized glutathione, the enzyme exhibits no oxidative activity Burkholderia pseudomallei ?
-
-

Synonyms

EC Number Synonyms Comment Organism
1.8.4.15 disulfide oxidoreductase
-
 Burkholderia pseudomallei
1.8.4.15 DsbA
-
 Burkholderia pseudomallei

General Information

EC Number General Information Comment Organism
1.8.4.15 metabolism the enzyme is responsible for catalyzing the formation of disulfide bonds in secreted and membrane-associated proteins Burkholderia pseudomallei
1.8.4.15 physiological function the enzyme is required for virulence of Burkholderia pseudomallei Burkholderia pseudomallei