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Information on EC 1.8.4.15 - protein dithiol oxidoreductase (disulfide-forming)
for references in articles please use BRENDA:EC1.8.4.15
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EC Tree 1 Oxidoreductases
1.8 Acting on a sulfur group of donors
1.8.4 With a disulfide as acceptor
1.8.4.15 protein dithiol oxidoreductase (disulfide-forming)
IUBMB Comments
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.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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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
Synonyms
disulfide oxidoreductase, ctdsba, msh-dependent thiol-disulfide reductase, c. trachomatis disulfide bond protein a, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C. trachomatis disulfide bond protein A
CtDsbA
DsbA
SdbA
Streptococcus disulfide bond protein A
TDOR
thiol-disulfide oxidoreductase
DsbA
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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
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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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
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
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
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
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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
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
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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
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
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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
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
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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
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
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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
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
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PATHWAY SOURCE
PATHWAYS
MetaCyc
cytochrome c biogenesis (system I type), periplasmic disulfide bond formation
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
7-amido-4-methylcoumarin-labelled cysteine pair-containing reporter peptide substrate + oxidized europium
?
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Substrates: -
Products: -
Products: -
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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
dithiothreitol + reduced bovine ribonuclease A
? + oxidized bovine ribonuclease A
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Substrates: -
Products: -
Products: -
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GSSG + reduced alkaline phosphatase
2 GSH + oxidized alkaline phosphatase
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Substrates: -
Products: -
Products: -
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insulin + a [protein] with reduced L-cysteine residues
?
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Substrates: -
Products: -
Products: -
?
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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Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
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a [DsbA protein] carrying a disulfide bond + N-acetylmuramidase/lysin AtlS
?
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Substrates: 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
Products: -
Products: -
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a [DsbA protein] carrying a disulfide bond + N-acetylmuramidase/lysin AtlS
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Substrates: 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
Products: -
Products: -
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additional information
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Substrates: in the absence of oxidized glutathione, the enzyme exhibits no oxidative activity
Products: -
Products: -
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additional information
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Substrates: membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA
Products: -
Products: -
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additional information
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Substrates: membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA
Products: -
Products: -
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additional information
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Substrates: membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA
Products: -
Products: -
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additional information
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurring via a dithiol mechanism
Products: -
Products: -
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additional information
?
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurring via a dithiol mechanism
Products: -
Products: -
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additional information
?
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurring via a dithiol mechanism
Products: -
Products: -
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additional information
?
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurring via a dithiol mechanism
Products: -
Products: -
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additional information
?
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurring via a dithiol mechanism
Products: -
Products: -
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additional information
?
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurring via a dithiol mechanism
Products: -
Products: -
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additional information
?
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurring via a dithiol mechanism
Products: -
Products: -
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additional information
?
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurring via a dithiol mechanism
Products: -
Products: -
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additional information
?
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Substrates: 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
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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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Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
a [DsbA protein] carrying a disulfide bond + N-acetylmuramidase/lysin AtlS
?
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Substrates: 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
Products: -
Products: -
?
a [DsbA protein] carrying a disulfide bond + N-acetylmuramidase/lysin AtlS
?
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Substrates: 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
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Oxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent infection and development.
Insulinoma
Thiol-protein disulfide oxidoreductase and peptidase activities in insulinoma tissue.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
enzyme CtDsbA is expressed early in the Chlamydial trachomatis developmental cycle
brenda
additional information
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enzyme CtDsbA is expressed early in the Chlamydial trachomatis developmental cycle
brenda
additional information
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enzyme CtDsbA is expressed early in the Chlamydial trachomatis developmental cycle
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brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
CtDsbA protein is detected in Chlamydia trachomatis inclusion vacuoles at 20 h post infection, with more detected at 32 and similar levels at 44 h post infection as the developmental cycle proceeds
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brenda
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CtDsbA protein is detected in Chlamydia trachomatis inclusion vacuoles at 20 h post infection, with more detected at 32 and similar levels at 44 h post infection as the developmental cycle proceeds
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brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
deletion of the ncgl2478 gene increases the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
metabolism
physiological function
additional information
evolution
while CtDsbA shares common structural and biochemical features with the DsbA-II group of DsbA proteins, especially, CtDsbA shares just 15% sequence identity with the canonical EcDsbA protein and approximately 20% sequence identity with other members of the structurally characterised DsbA-II class proteins that contain a second disulfide. The second disulfide of CtDsbA does not influence interaction with CtDsbB
evolution
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while CtDsbA shares common structural and biochemical features with the DsbA-II group of DsbA proteins, especially, CtDsbA shares just 15% sequence identity with the canonical EcDsbA protein and approximately 20% sequence identity with other members of the structurally characterised DsbA-II class proteins that contain a second disulfide. The second disulfide of CtDsbA does not influence interaction with CtDsbB
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metabolism
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the enzyme acts as a direct donor of disulfides to newly synthesized periplasmic proteins
metabolism
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the enzyme is required for production of disulfide-bonded proteins
metabolism
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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
metabolism
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the enzyme is responsible for catalyzing the formation of disulfide bonds in secreted and membrane-associated proteins
metabolism
the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway, see EC 5.3.4.1 and EC 1.8.1.15
metabolism
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the enzyme is required for production of disulfide-bonded proteins
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physiological function
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the enzyme directly catalyzes disulfide bond formation and also has a role in maintaining the bacterial periplasm oxidative
physiological function
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the enzyme is required for virulence of Burkholderia pseudomallei
physiological function
disulfide bond protein A (DsbA) is the primary oxidase in the disulfide oxidative pathway of bacteria. DsbA catalyses the introduction of disulfide bonds into reduced and folding proteins in concert with a membrane protein partner DsbB. DsbB uses a quinone cofactor as an electron acceptor, and together the DsbA-DsbB pair ultimately shuttle electrons from a reduced protein substrate to molecular oxygen via the respiratory pathway. CtDsbA is directly oxidised by CtDsbB, in a reaction in which both periplasmic cysteine pairs of CtDsbB are required for complete activity. Potential role of CtDsbA in chlamydial envelope disulfide bonding, and importance of disulfide crosslinking of the Chlamydia envelope in infection and Chlamydia development
physiological function
enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr, EC 1.8.1.15)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster
physiological function
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enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr, EC 1.8.1.15)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster
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physiological function
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enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr, EC 1.8.1.15)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster
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physiological function
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enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr, EC 1.8.1.15)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster
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physiological function
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enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr, EC 1.8.1.15)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster
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physiological function
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enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr, EC 1.8.1.15)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster
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physiological function
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disulfide bond protein A (DsbA) is the primary oxidase in the disulfide oxidative pathway of bacteria. DsbA catalyses the introduction of disulfide bonds into reduced and folding proteins in concert with a membrane protein partner DsbB. DsbB uses a quinone cofactor as an electron acceptor, and together the DsbA-DsbB pair ultimately shuttle electrons from a reduced protein substrate to molecular oxygen via the respiratory pathway. CtDsbA is directly oxidised by CtDsbB, in a reaction in which both periplasmic cysteine pairs of CtDsbB are required for complete activity. Potential role of CtDsbA in chlamydial envelope disulfide bonding, and importance of disulfide crosslinking of the Chlamydia envelope in infection and Chlamydia development
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physiological function
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enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr, EC 1.8.1.15)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster
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additional information
the classic DsbA structure consists of a thioredoxin domain and an inserted alpha-helical bundle domain. The enzyme's active site is a Cys-Xaa-Xaa-Cys motif located at the N-terminus of helix H1. The sequence of the Xaa-Xaa dipeptide modulates the redox character of the enzyme. The catalytic surface of the protein features 3 loops: loop 1, (linking helix H1 and beta-strand B3), loop 2 (linking helix H6 and beta-strand B4) which contains a highly conserved cis-Pro residue, and loop 3 (linking helix H7 and beta-strand B5.) Together these loops govern the enzyme's redox properties and its interactions with protein substrates. CtDsbA has a second, non-catalytic disulfide, in addition to the enzymatically critical active site disulfide, this non-catalytic disulfide staples H3 and H5 of the inserted alpha-helix domain. In mutant CtDsbB-CCSS periplasmic loop 2 Cys98 and Cys104 are mutated to serines, in the presence of CtDsbB-CCSS or CtDsbB-SSCC, CtDsbA catalysed oxidation of the peptide substrate is markedly reduced relative to wild-type CtDsbB, although oxidation proceeds more rapidly than observed for negative controls containing only buffer, or the wild-type CtDsbB variant alone. The disulfide bonds present in periplasmic loops P1 and P2 of CtDsbB are each required for complete oxidation of CtDsbA. The second disulfide of CtDsbA does not influence interaction with CtDsbB
additional information
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the classic DsbA structure consists of a thioredoxin domain and an inserted alpha-helical bundle domain. The enzyme's active site is a Cys-Xaa-Xaa-Cys motif located at the N-terminus of helix H1. The sequence of the Xaa-Xaa dipeptide modulates the redox character of the enzyme. The catalytic surface of the protein features 3 loops: loop 1, (linking helix H1 and beta-strand B3), loop 2 (linking helix H6 and beta-strand B4) which contains a highly conserved cis-Pro residue, and loop 3 (linking helix H7 and beta-strand B5.) Together these loops govern the enzyme's redox properties and its interactions with protein substrates. CtDsbA has a second, non-catalytic disulfide, in addition to the enzymatically critical active site disulfide, this non-catalytic disulfide staples H3 and H5 of the inserted alpha-helix domain. In mutant CtDsbB-CCSS periplasmic loop 2 Cys98 and Cys104 are mutated to serines, in the presence of CtDsbB-CCSS or CtDsbB-SSCC, CtDsbA catalysed oxidation of the peptide substrate is markedly reduced relative to wild-type CtDsbB, although oxidation proceeds more rapidly than observed for negative controls containing only buffer, or the wild-type CtDsbB variant alone. The disulfide bonds present in periplasmic loops P1 and P2 of CtDsbB are each required for complete oxidation of CtDsbA. The second disulfide of CtDsbA does not influence interaction with CtDsbB
additional information
the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1, EC 1.20.4.3) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
additional information
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the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1, EC 1.20.4.3) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
additional information
-
the classic DsbA structure consists of a thioredoxin domain and an inserted alpha-helical bundle domain. The enzyme's active site is a Cys-Xaa-Xaa-Cys motif located at the N-terminus of helix H1. The sequence of the Xaa-Xaa dipeptide modulates the redox character of the enzyme. The catalytic surface of the protein features 3 loops: loop 1, (linking helix H1 and beta-strand B3), loop 2 (linking helix H6 and beta-strand B4) which contains a highly conserved cis-Pro residue, and loop 3 (linking helix H7 and beta-strand B5.) Together these loops govern the enzyme's redox properties and its interactions with protein substrates. CtDsbA has a second, non-catalytic disulfide, in addition to the enzymatically critical active site disulfide, this non-catalytic disulfide staples H3 and H5 of the inserted alpha-helix domain. In mutant CtDsbB-CCSS periplasmic loop 2 Cys98 and Cys104 are mutated to serines, in the presence of CtDsbB-CCSS or CtDsbB-SSCC, CtDsbA catalysed oxidation of the peptide substrate is markedly reduced relative to wild-type CtDsbB, although oxidation proceeds more rapidly than observed for negative controls containing only buffer, or the wild-type CtDsbB variant alone. The disulfide bonds present in periplasmic loops P1 and P2 of CtDsbB are each required for complete oxidation of CtDsbA. The second disulfide of CtDsbA does not influence interaction with CtDsbB
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). G4NNC6_CHLT4
Chlamydia trachomatis serovar A (strain A2497)
282
0
32171
TrEMBL
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Q8NMK6_CORGL
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
245
0
27072
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
additional information
additional information
formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
additional information
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formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
additional information
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formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
-
additional information
-
formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
-
additional information
-
formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
-
additional information
-
formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
-
additional information
-
formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
-
additional information
-
formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
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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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C24S
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
C21S
additional information
additional information
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the melting temperatures (Tm) of reduced and oxidised CtDsbA are similar
additional information
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the melting temperatures (Tm) of reduced and oxidised CtDsbA are similar
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose CL-GB column chromatography and Sephacryl S-200 gel filtration
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recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
gene dsbA, recombinant expression of recombinant enzyme in Escherichia coli, coexpression with Chlamydia trachomatis dsbB
gene ncgl2478, quantitative real-time PCR analysis, sequence comparisons, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CtDsbA protein is detected in Chlamydia trachomatis inclusion vacuoles at 20 h post infection, with more detected at 32 and similar levels at 44 h post infection as the developmental cycle proceeds
ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
CtDsbA protein is detected in Chlamydia trachomatis inclusion vacuoles at 20 h post infection, with more detected at 32 and similar levels at 44 h post infection as the developmental cycle proceeds
CtDsbA protein is detected in Chlamydia trachomatis inclusion vacuoles at 20 h post infection, with more detected at 32 and similar levels at 44 h post infection as the developmental cycle proceeds
-
-
ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
-
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ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
-
-
ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
-
-
ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
-
-
ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
-
-
ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Antioxid. Redox Signal.
20
606-617
2014
Burkholderia pseudomallei
brenda
Zapun, A.; Creighton, T.; Bardwell, J.
The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo
Biochemistry
32
5083-5092
1993
Escherichia coli
brenda
Bardwell, J.; McGovern, K.; Beckwith, J.
Identification of a protein required for disulfide bond formation in vivo
Cell
67
581-589
1991
Escherichia coli
brenda
Akiyama, Y.; Kamitani, S.; Kusukawa, N.; Ito, K.
In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product
J. Biol. Chem.
267
22440-22445
1992
Escherichia coli
brenda
Bader, M.; Muse, W.; Zander, T.; Bardwell, J.
Reconstitution of a protein disulfide catalytic system
J. Biol. Chem.
273
10302-10307
1998
Escherichia coli
brenda
Davey, L.; Ng, C.; Halperin, S.; Lee, S.
Functional analysis of paralogous thiol-disulfide oxidoreductases in Streptococcus gordonii
J. Biol. Chem.
288
16416-16429
2013
Streptococcus gordonii, Streptococcus gordonii SecCR1
brenda
Christensen, S.; Halili, M.; Strange, N.; Petit, G.; Huston, W.; Martin, J.; McMahon, R.
Oxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent infection and development
PLoS ONE
14
e0222595
2019
Chlamydia trachomatis (G4NNC6), Chlamydia trachomatis, Chlamydia trachomatis A2497 (G4NNC6)
brenda
Guddat, L.; Bardwell, J.; Martin, J.
Crystal structures of reduced and oxidized DsbA Investigation of domain motion and thiolate stabilization
Structure
6
757-767
1998
Escherichia coli (P0AEG4)
brenda
Liu, Y.; Li, X.; Luo, J.; Su, T.; Si, M.; Chen, C.
A novel mycothiol-dependent thiol-disulfide reductase in Corynebacterium glutamicum involving oxidative stress resistance
3 Biotech
11
372
2021
Corynebacterium glutamicum (Q8NMK6), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q8NMK6), Corynebacterium glutamicum BCRC 11384 (Q8NMK6), Corynebacterium glutamicum DSM 20300 (Q8NMK6), Corynebacterium glutamicum JCM 1318 (Q8NMK6), Corynebacterium glutamicum LMG 3730 (Q8NMK6), Corynebacterium glutamicum NCIMB 10025 (Q8NMK6)
brenda
EXTERNAL LINKS (specific for EC-Number 1.8.4.15)
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Release 2023.1 (January 2023)
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