NAD(P) transhydrogenase
From Proteopedia
(Difference between revisions)
(19 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | <StructureSection load=' | + | <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. The reaction is coupled with proton translocation across the cell membrane while the enzyme undergoes conformational change. PTH uses FAD as cofactor. PTH is composed of 3 domains | + | '''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. |
+ | |||
+ | == Structural highlights == | ||
+ | PTH is composed of 3 domains:<br /> | ||
* Domain I binds NAD(+)/NADH.<br /> | * Domain I binds NAD(+)/NADH.<br /> | ||
* Domain II is a membrane-spanning domain.<br /> | * Domain II is a membrane-spanning domain.<br /> | ||
* Domain III binds NADP(+)/NADPH.<br /> | * Domain III binds NADP(+)/NADPH.<br /> | ||
- | PTH is composed of 2 subunits. | + | PTH is composed of 2 subunits. Subunit β contains domain III and part of II. The active site of PTH contains <scene name='57/571286/Cv/6'>NAD in domain I</scene> and <scene name='57/571286/Cv/7'>NADP in domain III</scene><ref>PMID:15323555</ref>. Water molecules are shown as red spheres. |
- | + | ||
- | == | + | |
- | + | ==3D structures of NAD(P) transhydrogenase== | |
- | + | [[NAD(P) transhydrogenase 3D structures]] | |
- | [[ | + | |
- | + | </StructureSection> | |
- | + | == References == | |
- | + | <references/> | |
- | [[ | + | [[Category:Topic Page]] |
- | + | ||
- | + |
Current revision
|
References
- ↑ 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