Information on EC 1.12.1.5 - hydrogen dehydrogenase [NAD(P)+]

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The expected taxonomic range for this enzyme is: Pyrococcus furiosus

EC NUMBER
COMMENTARY hide
1.12.1.5
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RECOMMENDED NAME
GeneOntology No.
hydrogen dehydrogenase [NAD(P)+]
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
H2 + NAD(P)+ = H+ + NAD(P)H
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
hydrogen production
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SYSTEMATIC NAME
IUBMB Comments
hydrogen:NAD(P)+ oxidoreductase
A nickel, iron, iron-sulfur protein. The enzyme from the archaeon Pyrococcus furiosus is part of a heterotetrameric complex where the alpha and delta subunits function as a hydrogenase while the beta and gamma subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.3, hydrogen dehydrogenase (NADP+).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
H+ + NADPH
H2 + NADP+
show the reaction diagram
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
show the reaction diagram
H2 + NAD+
H+ + NADH
show the reaction diagram
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-
-
r
H2 + NADP+
H+ + NADPH
show the reaction diagram
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-
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r
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
contains 0.83 FAD per mol enzyme
NADPH
[2Fe-2S]-center
[4Fe-4S]-center
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
contains 21 atoms iron per mol enzyme
Iron
-
contains 1 nickel-iron catalytic site and 6 iron-sulfur clusters, contains 23 iron atoms/heterotetramer
Ni2+
contains 0.9 atoms nickel per mol enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.23
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crude native enzyme, using methyl viologen as cosubstrate, at pH 8.4 and 80C
7.96
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crude recombinant enzyme, using methyl viologen as cosubstrate, at pH 8.4 and 80C
126
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recombinant enzyme after 24fold purification, using methyl viologen as cosubstrate, at pH 8.4 and 80C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
30000
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
39000
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
52000
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 90
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the native enzyme shows half-lives of 14 h at 90C under argon (H2 evolution), 21 h at 25C under air (H2 evolution), and 10 h at 90C under argon (H2 oxidation). The recombinant enzyme shows half-lives of 6 h at 90C under argon (H2 evolution), 25 h at 25C under air (H2 evolution), and 5 h at 90C under argon (H2 oxidation)
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE column chromatography, hydroxyapatite column chromatography, phenyl Sepharose column chromatography, and Superdex 200 gel filtration
Strep-tag II column chromatography
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis