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Purification and enzymatic activity of an NADH‐fumarate reductase and other mitochondrial activities of Leishmania parasites
Author(s) -
CHEN M.,
BENNEDSEN M.,
ZHAI L.,
KHARAZMI A.
Publication year - 2001
Publication title -
apmis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0903-4641
DOI - 10.1034/j.1600-0463.2001.091201.x
Subject(s) - fumarate reductase , leishmania donovani , succinate dehydrogenase , biochemistry , reductase , enzyme , biology , fumarase , malate dehydrogenase , leishmania , mitochondrion , respiratory chain , citrate synthase , thioredoxin reductase , parasite hosting , leishmaniasis , visceral leishmaniasis , thioredoxin , world wide web , computer science , immunology
A 65 kD membrane‐associated NADH‐fumarate reductase subunit, which has a molecular weight similar to that of one of the enzyme subunits from bacteria, was purified from Leishmania donovani promastigotes. NADH‐fumarate reductase and other mitochondrial enzymatic activities of L. major and L. donovani promastigotes and amastigotes were investigated. The presence of NADH‐fumarate reductase was demonstrated in digitonin‐permeabilized L. major promastigotes and mitochondria of L. major and L. donovani promastigotes and amastigotes. The activity of solubilized NADH‐fumarate reductase was measured in L. major and L. donovani promastigotes. Succinate exhibited a clear concentration‐dependent inhibitory effect on fumarate reductase, whereas fumarate also exhibited a clear concentration‐dependent inhibitory effect on succinate dehydrogenase. The data indicate that fumarate reductase is an obligatory component of the respiratory chain of the parasite. Since the enzyme is an important component in the intermediate metabolism in the Leishmania parasite and is absent in mammalian cells, it could be a potential target for antileishmanial drugs.