NAD(P) transhydrogenase

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<StructureSection load='1u2d' size='450' side='right' caption='Structure of PTH domains I (cyan and green) and III (pink) complex with NAD, NADP and glycerol (PDB entry [[1u2d]])' scene='57/571286/Cv/1'>
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<StructureSection load='' size='450' side='right' caption='Structure of PTH domains I (cyan and green) and III (pink) complex with NAD, NADP and glycerol (PDB entry [[1u2d]])' scene='57/571286/Cv/1'>
'''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<ref>PMID:12788487</ref>. PTH uses FAD as cofactor.
'''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<ref>PMID:12788487</ref>. PTH uses FAD as cofactor.

Revision as of 15:45, 17 August 2017

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

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3D structures of NAD(P) transhydrogenase

Updated on 17-August-2017

References

  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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