EC Number   |
Substrates |
Organism |
Products |
Reversibility  |
|---|
   5.3.4.1 | more |
TXNDC5 directly interacts with Srx through its thioredoxin-like domains, binding and in vivo complexing analysis. The Srx-TXNDC5 interaction is not affected by the treatment of cells with exogenous H2O2 |
Homo sapiens |
? |
- |
- |
| 5.3.4.1 | more |
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 occurred via a dithiol mechanism |
Corynebacterium glutamicum |
? |
- |
- |
| 5.3.4.1 | more |
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 occurred via a dithiol mechanism |
Corynebacterium glutamicum LMG 3730 |
? |
- |
- |
| 5.3.4.1 | more |
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 occurred via a dithiol mechanism |
Corynebacterium glutamicum BCRC 11384 |
? |
- |
- |
| 5.3.4.1 | more |
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 occurred via a dithiol mechanism |
Corynebacterium glutamicum ATCC 13032 |
? |
- |
- |
| 5.3.4.1 | more |
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 occurred via a dithiol mechanism |
Corynebacterium glutamicum JCM 1318 |
? |
- |
- |
| 5.3.4.1 | more |
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 occurred via a dithiol mechanism |
Corynebacterium glutamicum NCIMB 10025 |
? |
- |
- |
| 5.3.4.1 | more |
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 occurred via a dithiol mechanism |
Corynebacterium glutamicum DSM 20300 |
? |
- |
- |
| 5.3.4.1 | Agp mutant |
folding of Agp mutant, DsbC, mutant of Agp, an AppA homologue, containing the AppA nonconsecutive disulfide bond |
Escherichia coli |
? |
- |
? |
| 5.3.4.1 | alkaline protease inhibitor |
folding and rearrangement of alkaline protease inhibitor |
Streptomyces sp. |
? |
- |
? |
