Abstract
We have expressed and purified a protein fragment from Entamoeba histolytica. It catalyses transhydrogenation between analogues of NAD(H) and NADP(H). The characteristics of this reaction resemble those of the reaction catalysed by a complex of the NAD(H)- and NADP(H)-binding subunits of proton-translocating transhydrogenases from bacteria and mammals. It is concluded that the complete En. histolytica protein, which, along with similar proteins from other protozoan parasites, has an unusual subunit organisation, is also a proton-translocating transhydrogenase. The function of the transhydrogenase, thought to be located in organelles which do not have the enzymes of oxidative phosphorylation, is not clear. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
| Original language | English |
|---|---|
| Pages (from-to) | 51-54 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 488 |
| Issue number | 1-2 |
| DOIs | |
| Publication status | Published - 12 Jan 2001 |
Keywords
- hydride transfer
- Entamoeba histolytica
- proton pump
- nucleotide binding
- protozoan parasite
- transhydrogenase