EC 1.12.1.3 - Hydrogen dehydrogenase (NADP+)

  IntEnz view ENZYME view
XML

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]
Systematic name:
hydrogen:NADP+ oxidoreductase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050583
CAS Registry Number: 9027-05-8
UniProtKB/Swiss-Prot:

References

  1. de Luca, G., de Philip, P., Rousset, M., Belaich, J.P. and Dermoun, Z.
    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]
  2. Bryant, F. O., Adams, M. W.
    Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus.
    J. Biol. Chem. 264 : 5070-5079 (1989). [PMID: 2538471]
  3. Ma, K., Schicho, R. N., Kelly, R. M., Adams, M. W.
    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]
  4. Ma, K., Zhou, Z.H. and Adams, M.W.
    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).
  5. van Haaster, D. J., Silva, P. J., Hagedoorn, P. L., Jongejan, J. A., Hagen, W. R.
    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]