The membrane-peripheral subunits of transhydrogenase from Entamoeba histolytica are functional only when dimerized

Unlike their bacterial and mammalian counterparts, the NADP(H)- and NAD(H)-binding components of proton-translocating transhydrogenase from the protozoan parasite Entamoeba histolytica (denoted ehdIII and ehdI, respectively) are tethered by a polypeptide linker. The recombinant tethered fragment, eh...

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Veröffentlicht in:	The Journal of biological chemistry 2002-07, Vol.277 (29), p.26163-26170
Hauptverfasser:	Weston, Chris J, Venning, Jamie D, Jackson, J Baz
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Dimerization Entamoeba histolytica - enzymology NAD - metabolism NADP - metabolism NADP Transhydrogenases - physiology Protein Conformation Scattering, Radiation Structure-Activity Relationship
Online-Zugang:	Volltext
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