The unusal transhydrogenase of Entamoeba histolytica

Research output: Contribution to journalArticle

Standard

The unusal transhydrogenase of Entamoeba histolytica. / Weston, Christopher; White, Scott; Jackson, John.

In: FEBS Letters, Vol. 488, No. 1-2, 12.01.2001, p. 51-54.

Research output: Contribution to journalArticle

Harvard

APA

Vancouver

Author

Bibtex

@article{dca91f92633c4cd5940f63a440a9495b,
title = "The unusal transhydrogenase of Entamoeba histolytica",
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.",
keywords = "hydride transfer, Entamoeba histolytica, proton pump, nucleotide binding, protozoan parasite, transhydrogenase",
author = "Christopher Weston and Scott White and John Jackson",
year = "2001",
month = jan,
day = "12",
doi = "10.1016/S0014-5793(00)02386-3",
language = "English",
volume = "488",
pages = "51--54",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "1-2",

}

RIS

TY - JOUR

T1 - The unusal transhydrogenase of Entamoeba histolytica

AU - Weston, Christopher

AU - White, Scott

AU - Jackson, John

PY - 2001/1/12

Y1 - 2001/1/12

N2 - 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.

AB - 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.

KW - hydride transfer

KW - Entamoeba histolytica

KW - proton pump

KW - nucleotide binding

KW - protozoan parasite

KW - transhydrogenase

UR - http://www.scopus.com/inward/record.url?scp=0035846860&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(00)02386-3

DO - 10.1016/S0014-5793(00)02386-3

M3 - Article

C2 - 11163794

VL - 488

SP - 51

EP - 54

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1-2

ER -