EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.12.1.2 | additional information | at a redox potential of approx. -100 mV the inactive form of the enzyme is transformed into an active one | Cupriavidus necator |
EC Number | General Stability | Organism |
---|---|---|
1.12.1.2 | oxidized inactive form of the enzyme is the most stable against thermodenaturation, proteolysis, and inactivation in urea | Cupriavidus necator |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.12.1.2 | Cupriavidus necator | - |
- |
- |
1.12.1.2 | Cupriavidus necator | - |
formerly Alcaligenes eutrophus | - |
1.12.1.2 | Cupriavidus necator Z1 | - |
- |
- |
EC Number | Oxidation Stability | Organism |
---|---|---|
1.12.1.2 | redox-dependent inactivation and activation, proposed inactivation mechanism | Cupriavidus necator |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.12.1.2 | H2 + NAD+ = H+ + NADH | catalytic activity may be regulated by the reduction of a regulatory center followed by a series of structural changes | Cupriavidus necator |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.12.1.2 | H2 + NAD+ | - |
Cupriavidus necator | H+ + NADH | - |
? | |
1.12.1.2 | H2 + NAD+ | - |
Cupriavidus necator Z1 | H+ + NADH | - |
? |