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The unusual transhydrogenase of Entamoeba histolytica
Author(s) -
Weston Chris J.,
White Scott A.,
Jackson J.Baz
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02386-3
Subject(s) - entamoeba histolytica , nad+ kinase , oxidative phosphorylation , entamoeba , protein subunit , biochemistry , enzyme , chemistry , organelle , biology , microbiology and biotechnology , gene
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.