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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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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-
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r
H2 + NADP+
H+ + NADPH
show the reaction diagram
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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
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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 80°C
7.96
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crude recombinant enzyme, using methyl viologen as cosubstrate, at pH 8.4 and 80°C
126
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recombinant enzyme after 24fold purification, using methyl viologen as cosubstrate, at pH 8.4 and 80°C
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 90°C under argon (H2 evolution), 21 h at 25°C under air (H2 evolution), and 10 h at 90°C under argon (H2 oxidation). The recombinant enzyme shows half-lives of 6 h at 90°C under argon (H2 evolution), 25 h at 25°C under air (H2 evolution), and 5 h at 90°C 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