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Literature summary for 1.12.1.2 extracted from

  • Tikhonova, T.V.; Savel'eva, N.D.; Popov, V.O.
    Chemical modification of catalytically essential functional groups of NAD-dependent hydrogenase from Ralstonia eutropha H16 (2003), Biochemistry, 68, 994-1001.
    View publication on PubMed

Inhibitors

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 [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Cupriavidus necator

Metals/Ions

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

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 [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2030
-
purified hydrogenase, at 30°C Cupriavidus necator

Substrates and Products (Substrate)

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

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

Synonyms Comment Organism
NAD-dependent hydrogenase
-
Cupriavidus necator

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
assay at Cupriavidus necator

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.9
-
assay at Cupriavidus necator

Cofactor

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