ExplorEnz: EC 1.6.1.3

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1.6.1.3

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 7.1.1.1, proton-translocating NAD(P)⁺ transhydrogenase. This entry stands for enzymes whose stereo-specificity with respect to NADPH is not known. [cf. EC 1.6.1.1, NAD(P)⁺ transhydrogenase (Si-specific)].

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc

References:

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 1.6.1.3 created 2013]