EC 1 - Oxidoreductases
EC 1.12 - Acting on hydrogen as donors
EC 1.12.1 - With NAD+ or NADP+ as acceptor
EC 1.12.1.3 - Hydrogen dehydrogenase (NADP+)
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.12.1.3
Names
Accepted name:
hydrogen dehydrogenase (NADP+)
Other
names:
NADP+-linked hydrogenase
NADP+-reducing hydrogenase
hydrogenase [ambiguous]
hydrogenase I [ambiguous]
NADP+-reducing hydrogenase
hydrogenase [ambiguous]
hydrogenase I [ambiguous]
Systematic name:
hydrogen:NADP+ oxidoreductase
Reaction
- H2 + NADP+ = H+ + NADPH
Cofactors
Comments:
The protein from the bacterium Desulfovibrio fructosovorans is an iron-sulfur protein that exclusively functions as a hydrogen dehydrogenase, while the enzyme from the archaeon Pyrococcus furiosus is a nickel, iron, iron-sulfur protein, that is part of a heterotetrameric complex where the α and δ subunits function as a hydrogenase while the β and γ subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.5, hydrogen dehydrogenase [NAD(P)+].
Links to other databases
Gene Ontology:
GO:0050583
CAS Registry Number:
9027-05-8
UniProtKB/Swiss-Prot:
HNDA_DESFR
HNDB_DESFR
HNDC_DESFR
HNDD_DESFR
HYD1A_PYRFU
HYD1D_PYRFU
References
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The NADP-reducing hydrogenase of Desulfovibrio fructosovorans: Evidence for a native complex with hydrogen-dependent methyl-viologen-reducing activity.Biochem. Biophys. Res. Commun. 248 : 591-596 (1998). [PMID: 9703971]
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Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus.J. Biol. Chem. 264 : 5070-5079 (1989). [PMID: 2538471]
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Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor.Proc. Natl. Acad. Sci. U.S.A. 90 : 5341-5344 (1993). [PMID: 8389482]
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Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus: A key role for NADPH.FEMS Microbiol. Lett. 122 : 245-250 (1994).
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Reinvestigation of the steady-state kinetics and physiological function of the soluble NiFe-hydrogenase I of Pyrococcus furiosus.J. Bacteriol. 190 : 1584-1587 (2008). [PMID: 18156274]
[EC 1.12.1.3 created 2002, modified 2013]