The Enzyme Database

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Accepted name: NAD(P)+ transhydrogenase
Reaction: NADPH + NAD+ = NADP+ + NADH
Other name(s): soluble transhydrogenase; pyridine nucleotide transhydrogenase; transhydrogenase (ambiguous); nicotinamide adenine dinucleotide (phosphate) transhydrogenase (ambiguous); NAD+ transhydrogenase (ambiguous); NADH transhydrogenase (misleading); nicotinamide nucleotide transhydrogenase (ambiguous); NADPH-NAD+ transhydrogenase (ambiguous); pyridine nucleotide transferase (ambiguous); NADPH-NAD+ oxidoreductase (ambiguous); NADH-NADP+-transhydrogenase (ambiguous); NADPH:NAD+ transhydrogenase; H+-Thase (ambiguous); non-energy-linked transhydrogenase (ambiguous); sthA (gene name)
Systematic name: NADPH:NAD+ oxidoreductase
Comments: A flavoprotein (FAD). The main function of the enzyme is to oxidize excess of NADPH, forming NADH that supplies electrons to the respiratory chain. cf. EC, proton-translocating NAD(P)+ transhydrogenase. This entry stands for enzymes whose stereo-specificity with respect to NADPH is not known. [cf. EC, NAD(P)+ transhydrogenase (Si-specific)].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc
1.  Keister D.L., San Pietro A., Stolzenbach F.E. Pyridine nucleotide transhydrogenase from spinach. I. Purification and properties. J. Biol. Chem. 235 (1960) 2989–2996. [DOI] [PMID: 13752224]
2.  Sauer, U., Canonaco, F., Heri, S., Perrenoud, A. and Fischer, E. The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli. J. Biol. Chem. 279 (2004) 6613–6619. [DOI] [PMID: 14660605]
3.  Zhao, H., Wang, P., Huang, E., Ge, Y. and Zhu, G. Physiologic roles of soluble pyridine nucleotide transhydrogenase in Escherichia coli as determined by homologous recombination. Ann Microbiol 58 (2008) 275–280. [DOI]
4.  Cao, Z., Song, P., Xu, Q., Su, R. and Zhu, G. Overexpression and biochemical characterization of soluble pyridine nucleotide transhydrogenase from Escherichia coli. FEMS Microbiol. Lett. 320 (2011) 9–14. [DOI] [PMID: 21545646]
5.  Partipilo, M., Yang, G., Mascotti, M.L., Wijma, H.J., Slotboom, D.J. and Fraaije, M.W. A conserved sequence motif in the Escherichia coli soluble FAD-containing pyridine nucleotide transhydrogenase is important for reaction efficiency. J. Biol. Chem. 298:102304 (2022). [DOI] [PMID: 35933012]
[EC created 2013]

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