The Enzyme Database

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Accepted name: hydrogen dehydrogenase (NADP+)
Reaction: H2 + NADP+ = H+ + NADPH
Other name(s): NADP+-linked hydrogenase; NADP+-reducing hydrogenase; hydrogenase (ambiguous); hydrogenase I (ambiguous)
Systematic name: hydrogen:NADP+ oxidoreductase
Comments: The protein from the bacterium Desulfovibrio fructosovorans is an iron-sulfur protein that exclusively functions as a hydrogen dehydrogenase [1], 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, sulfhydrogenase). Different from EC, hydrogen dehydrogenase [NAD(P)+].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-05-8
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 (1998) 591–596. [DOI] [PMID: 9703971]
2.  Bryant, F.O. and Adams, M.W. Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus. J. Biol. Chem. 264 (1989) 5070–5079. [PMID: 2538471]
3.  Ma, K., Schicho, R.N., Kelly, R.M. and 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. USA 90 (1993) 5341–5344. [DOI] [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 (1994) 245–250.
5.  van Haaster, D.J., Silva, P.J., Hagedoorn, P.L., Jongejan, J.A. and Hagen, W.R. Reinvestigation of the steady-state kinetics and physiological function of the soluble NiFe-hydrogenase I of Pyrococcus furiosus. J. Bacteriol. 190 (2008) 1584–1587. [DOI] [PMID: 18156274]
[EC created 2002, modified 2013]

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