NAD(P) transhydrogenase
From Proteopedia
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(New page: <StructureSection load='2bru' size='350' side='right' caption='Structure of E. coli PTH domains I and III complex with NAD and NADP (PDB entry 2bru)' scene=''> '''NAD(P) transhyd...) |
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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'> | ||
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+ | '''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 /> | |
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* 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. |
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- | == | + | |
- | + | ==3D structures of NAD(P) transhydrogenase== | |
- | + | [[NAD(P) transhydrogenase 3D structures]] | |
- | [[ | + | |
- | + | </StructureSection> | |
- | + | == References == | |
- | + | <references/> | |
- | [[ | + | [[Category:Topic Page]] |
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Current revision
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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