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Literature summary for 1.8.4.15 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
Search for more literature for 1.8.4.15

Activating Compound

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

Cloned(Commentary)

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

Organism

Organism UniProt Comment Textmining
Burkholderia pseudomallei
-
-
-

Purification (Commentary)

Purification (Comment) Organism
immobilized metal affinity chromatography Burkholderia pseudomallei

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
disulfide oxidoreductase
-
 Burkholderia pseudomallei
DsbA
-
 Burkholderia pseudomallei

General Information

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