EC Number | Cloned (Comment) | Organism |
---|---|---|
1.8.1.14 | expressed in Escherichia coli BL21(DE3)pLysS cells | Pyrococcus horikoshii |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.8.1.14 | hanging drop and sitting drop vapor diffusion methods, using 100 mM Tris, pH 8.0, 2-3 M 1,6-hexanediol, and 200 mM MgCl2 | Pyrococcus horikoshii |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.8.1.14 | 0.009 | - |
NADPH | at 50°C and pH 8.1 in 1 M Tris buffer | Pyrococcus horikoshii | |
1.8.1.14 | 0.073 | - |
NADPH | at 50°C and pH 8.1 in 1 M Tris buffer | Pyrococcus horikoshii |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.1.14 | CoA-disulfide + NADH + H+ | Pyrococcus horikoshii | - |
CoA + NAD+ | - |
? | |
1.8.1.14 | CoA-disulfide + NADPH + H+ | Pyrococcus horikoshii | - |
CoA + NADP+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.8.1.14 | Pyrococcus horikoshii | O58308 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.8.1.14 | Ni-NTA column chromatography | Pyrococcus horikoshii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.1.14 | CoA-disulfide + NADH + H+ | - |
Pyrococcus horikoshii | CoA + NAD+ | - |
? | |
1.8.1.14 | CoA-disulfide + NADPH + H+ | - |
Pyrococcus horikoshii | CoA + NADP+ | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.8.1.14 | CoADR | - |
Pyrococcus horikoshii |
1.8.1.14 | coenzyme A disulfide reductase | - |
Pyrococcus horikoshii |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.8.1.14 | 7.2 | - |
NADPH | at 50°C and pH 8.1 in 1 M Tris buffer | Pyrococcus horikoshii | |
1.8.1.14 | 8.1 | - |
NADPH | at 50°C and pH 8.1 in 1 M Tris buffer | Pyrococcus horikoshii |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.8.1.14 | coenzyme A | - |
Pyrococcus horikoshii | |
1.8.1.14 | FAD | - |
Pyrococcus horikoshii | |
1.8.1.14 | NADH | - |
Pyrococcus horikoshii | |
1.8.1.14 | NADPH | the enzyme shows a preference for NADPH (10fold lower Km), although it makes efficient use of NADH as well | Pyrococcus horikoshii |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.8.1.14 | physiological function | the enzyme is not essential for S0 respiration in Pyrococcus but appears to participate in oxidative defense in the presence of elemental sulfur | Pyrococcus horikoshii |