S. Marche et al., Comparative study of Leishmania mexicana and Trypanosoma brucei NAD-dependent glycerol-3-phosphate dehydrogenase, MOL BIOCH P, 106(1), 2000, pp. 83-91
The NAD-dependent glycerol-3-phosphate dehydrogenases (G3PDH EC 1.1.1.8) of
Trypanosoma brucei and Leishmania mexicana ale thought to have different r
oles in carbohydrate metabolism. Here the physicochemical and kinetic prope
rties of natural G3PDH from T. brucei with the recombinant homologue of L.
mexicana which share 63% positional identity ale compared. Despite their su
pposed different functions in energy metabolism of the parasites the two G3
PDHs have remarkably similar properties, including pH optima and K-m value
for dihydroxyacetone phosphate (DHAP) and NADH in the formation of glycerol
3-phosphate (G3P) and for NAD(+) and G3P in the reverse reaction. Both enz
ymes are subject to substrate inhibition by dihydroxyacetone phosphate at c
oncentrations above 0.2 mM and are inhibited by the trypanocidal drugs sura
min and melarsen oxide at sub-micromolar concentrations. (C) 2000 Elsevier
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