1.8.4.15: protein dithiol oxidoreductase (disulfide-forming)
This is an abbreviated version!
For detailed information about protein dithiol oxidoreductase (disulfide-forming), go to the full flat file.
Reaction
Synonyms
C. trachomatis disulfide bond protein A, CtDsbA, disulfide oxidoreductase, DsbA, More, MSH-dependent thiol-disulfide reductase, mycothiol-dependent thiol-disulfide reductase, ncgl2478, protein dithiol oxidoreductase, SdbA, Streptococcus disulfide bond protein A, TDOR, thiol-disulfide oxidoreductase
ECTree
1.8.4.15 protein dithiol oxidoreductase (disulfide-forming)Advanced search results
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results (Substrates Products
Substrates Products on EC 1.8.4.15 - protein dithiol oxidoreductase (disulfide-forming)
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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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-
?
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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-
-
-
?
GSSG + reduced alkaline phosphatase
2 GSH + oxidized alkaline phosphatase
-
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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
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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
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-
?
a [DsbA protein] carrying a disulfide bond + N-acetylmuramidase/lysin AtlS
?
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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
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?
a [DsbA protein] carrying a disulfide bond + N-acetylmuramidase/lysin AtlS
?
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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
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?
additional information
?
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in the absence of oxidized glutathione, the enzyme exhibits no oxidative activity
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additional information
?
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membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA
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additional information
?
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membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA
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additional information
?
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membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA
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-
additional information
?
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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
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additional information
?
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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
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-
additional information
?
-
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
-
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additional information
?
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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
-
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additional information
?
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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
-
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-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
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additional information
?
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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
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