NAD(P) transhydrogenase
From Proteopedia
(Difference between revisions)
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| - | <StructureSection load='1u2d' size=' | + | <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'> |
'''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. | ||
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* 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. Subunit β contains domain III and part of II. The active site of PTH contains NAD in domain I and NADP in domain III<ref>PMID:15323555</ref>. | + | 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/3'>NAD in domain I</scene> and <scene name='57/571286/Cv/5'>NADP in domain III</scene><ref>PMID:15323555</ref>. Water molecules shown as red spheres. |
</StructureSection> | </StructureSection> | ||
Revision as of 09:57, 30 May 2016
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3D structures of NAD(P) transhydrogenase
Updated on 30-May-2016
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
