Inhibitors | Comment | Organism | Structure |
---|---|---|---|
diethyl dicarbonate | chemical modification of active site His residues results in reduced enzymatic hydrogenase and diaphorase activities, pH-dependence and kinetics of modifications/inactivation | Cupriavidus necator | |
DTNB | modification of thiol groups of activated enzyme results in rapid inactivation of both activities, modification of the residues of nonactivated enzyme has small effects on the enzyme activities, pH-dependence and kinetics of modifications/inactivation | Cupriavidus necator | |
iodoacetic acid | modification of thiol groups of activated enzyme results in rapid inactivation of both activities, modification of the residues of nonactivated enzyme has small effects on the enzyme activities, pH-dependence and kinetics of modifications/inactivation | Cupriavidus necator |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Cupriavidus necator |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | the diaphorase contains 3 [2Fe-2S] cluster, the hydrogenase subunit HoxY contains one [2Fe-2S] cluster coordinated by 9 Cys residues | Cupriavidus necator | |
Mg2+ | bound to the hydrogenase subunits | Cupriavidus necator | |
Ni2+ | enzyme contains a [Ni-Fe] cluster | Cupriavidus necator |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cupriavidus necator | - |
heterotetrameric multifunctional enzyme showing both hydrogenase and diaphorase activities | - |
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | - |
heterotetrameric multifunctional enzyme showing both hydrogenase and diaphorase activities | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
2030 | - |
purified hydrogenase, at 30°C | Cupriavidus necator |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ferrocyanide + NAD+ | - |
Cupriavidus necator | ferricyanide + NADH | - |
r | |
ferrocyanide + NAD+ | - |
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | ferricyanide + NADH | - |
r | |
H2 | hydrogenase reaction part | Cupriavidus necator | H+ + e- | - |
r | |
H2 | hydrogenase reaction part | Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | H+ + e- | - |
r | |
H2 + ferricyanide | - |
Cupriavidus necator | H+ + ferrocyanide | - |
r | |
H2 + ferricyanide | - |
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | H+ + ferrocyanide | - |
r | |
H2 + NAD+ | overall reaction | Cupriavidus necator | H+ + NADH | - |
r | |
H2 + NAD+ | overall reaction | Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | H+ + NADH | - |
r | |
additional information | enzyme shows both hydrogenase and diaphorase activities, proton channeling | Cupriavidus necator | ? | - |
? | |
additional information | enzyme shows both hydrogenase and diaphorase activities, proton channeling | Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | ? | - |
? | |
NAD+ + H+ + e- | diaphorase reaction part | Cupriavidus necator | NADH | - |
r |
Subunits | Comment | Organism |
---|---|---|
oligomer | heterotetrameric multifunctional enzyme showing both hydrogenase and diaphorase activities, subunits HoxHY form a heterodimer which is responsible for the hydrogenase activity with 56 kDa for HoxH and 26 kDa for HoxY, subunits HoxFU form a heterodimer which is responsible for the NADH-dehydrogenase, i.e. diaphorase activity | Cupriavidus necator |
Synonyms | Comment | Organism |
---|---|---|
NAD-dependent hydrogenase | - |
Cupriavidus necator |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | - |
assay at | Cupriavidus necator |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.9 | - |
assay at | Cupriavidus necator |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FMN | bound to the diaphorase subunits | Cupriavidus necator | |
NAD+ | dependent on, binding site on the diaphorase subunits | Cupriavidus necator | |
NADH | dependent on, binding site on the diaphorase subunits | Cupriavidus necator |