NAD(P) transhydrogenase

NAD(P) transhydrogenase (PTH) catalyzes the conversion of NADP and NADH to NADPH and NAD. See NAD and NAD(P)H. The reaction is coupled with proton translocation across the cell membrane while the enzyme undergoes conformational change^[1]. PTH uses FAD as cofactor.

Structural highlights

PTH is composed of 3 domains:

Domain I binds NAD(+)/NADH.
Domain II is a membrane-spanning domain.
Domain III binds NADP(+)/NADPH.

PTH is composed of 2 subunits. Subunit β contains domain III and part of II. The active site of PTH contains and ^[2]. Water molecules are shown as red spheres.

3D structures of NAD(P) transhydrogenase

NAD(P) transhydrogenase 3D structures

Structure of PTH domains I (cyan and green) and III (pink) complex with NAD, NADP and glycerol (PDB entry 1u2d)

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Jackson JB. Proton translocation by transhydrogenase. FEBS Lett. 2003 Jun 12;545(1):18-24. PMID:12788487
↑ Mather OC, Singh A, van Boxel GI, White SA, Jackson JB. Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase. Biochemistry. 2004 Aug 31;43(34):10952-64. PMID:15323555 doi:10.1021/bi0497594

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Michal Harel, Alexander Berchansky, Joel L. Sussman

[1] Jackson JB. Proton translocation by transhydrogenase. FEBS Lett. 2003 Jun 12;545(1):18-24. PMID:12788487

[2] Mather OC, Singh A, van Boxel GI, White SA, Jackson JB. Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase. Biochemistry. 2004 Aug 31;43(34):10952-64. PMID:15323555 doi:10.1021/bi0497594

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