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Literature summary extracted from

  • Lauterbach, L.; Idris, Z.; Vincent, K.; Lenz, O.
    Catalytic properties of the isolated diaphorase fragment of the NAD +-reducing [NiFe]-hydrogenase from Ralstonia eutropha (2011), PLoS ONE, 6, e25939.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.12.1.2 NAD+ product inhibition; product inhibition Cupriavidus necator
1.12.1.2 NADH product inhibition; product inhibition Cupriavidus necator

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.12.1.2 0.056
-
 NADH pH 8.0, temperature not specified in the publication Cupriavidus necator
1.12.1.2 0.197
-
 NAD+ pH 8.0, temperature not specified in the publication Cupriavidus necator

Organism

EC Number Organism UniProt Comment Textmining
1.12.1.2 Cupriavidus necator P22317 subunit alpha
-
1.12.1.2 Cupriavidus necator P22318 subunit gamma
-
1.12.1.2 Cupriavidus necator DSM 428 P22317 subunit alpha
-
1.12.1.2 Cupriavidus necator DSM 428 P22318 subunit gamma
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.12.1.2 H+ + NADH module HoxFU shows clear electrocatalytic activity for both NAD+ reduction and NADH oxidation with minimal overpotential relative to the potential of the NAD+/NADH couple Cupriavidus necator H2 + NAD+
-
 r
1.12.1.2 H+ + NADH module HoxFU shows clear electrocatalytic activity for both NAD+ reduction and NADH oxidation with minimal overpotential relative to the potential of the NAD+/NADH couple Cupriavidus necator DSM 428 H2 + NAD+
-
 r
1.12.1.2 H2 + NAD+ module HoxFU shows clear electrocatalytic activity for both NAD+ reduction and NADH oxidation with minimal overpotential relative to the potential of the NAD+/NADH couple Cupriavidus necator H+ + NADH
-
 r
1.12.1.2 H2 + NAD+ module HoxFU shows clear electrocatalytic activity for both NAD+ reduction and NADH oxidation with minimal overpotential relative to the potential of the NAD+/NADH couple Cupriavidus necator DSM 428 H+ + NADH
-
 r
1.12.1.2 additional information in protein film electrochemical experiments the electrocatalytic current is unaffected by O2. In aerobic solution assays, a moderate superoxide production rate of 54 nmol per mg of protein is observed, meaning that the formation of reactive oxygen species observed for the native enzyme can be attributed mainly to module HoxFU Cupriavidus necator ?
-
 ?
1.12.1.2 additional information in protein film electrochemical experiments the electrocatalytic current is unaffected by O2. In aerobic solution assays, a moderate superoxide production rate of 54 nmol per mg of protein is observed, meaning that the formation of reactive oxygen species observed for the native enzyme can be attributed mainly to module HoxFU Cupriavidus necator DSM 428 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.12.1.2 HoxF
-
 Cupriavidus necator
1.12.1.2 HoxU
-
 Cupriavidus necator

Cofactor

EC Number Cofactor Comment Organism Structure
1.12.1.2 FMN module HoxFU accommodates a [2Fe2S] cluster, FMN and a series of [4Fe4S] clusters Cupriavidus necator
1.12.1.2 [2Fe-2S]-center HoxFU accommodates a [2Fe2S] cluster, FMN and a series of [4Fe4S] clusters Cupriavidus necator
1.12.1.2 [4Fe-4S]-center HoxFU accommodates a [2Fe2S] cluster, FMN and a series of [4Fe4S] clusters Cupriavidus necator

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.12.1.2 0.2
-
 NAD+ pH 8.0, temperature not specified in the publication Cupriavidus necator
1.12.1.2 0.2
-
 NADH pH 8.0, temperature not specified in the publication Cupriavidus necator