Dihydrolipoamide dehydrogenase has been discovered in the bloodstream form of the eukaryotic African parasite, Trypanosoma brucei. The enzyme catalysed the stoichiometric oxidation of dihydrolipoamide by NAD+ and exhibited a hyperbolic dependence of catalytic activity on the concentrations of both dihydrolipoamide and NAD+. Chemical modification with the tervalent arsenical reagent p-aminophenyldichloroarsine indicates the involvement in catalysis of a reversibly reducible disulphide bond. Plasma-membrane sheets were purified from T. brucei, and it was shown that virtually all the dihydrolipoamide dehydrogenase remained closely associated with this membrane preparation. T. brucei apparently lacks the 2-oxoacid dehydrogenase multienzyme complexes of which dihydrolipoamide dehydrogenase is usually an integral component. In the context of this absence, the possible function of trypanosomal dihydrolipoamide dehydrogenase is discussed, with particular reference to its cellular location in the plasma membrane.
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May 1987
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Research Article|
May 01 1987
Dihydrolipoamide dehydrogenase from Trypanosoma brucei. Characterization and cellular location
M J Danson
;
M J Danson
*Department of Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, U.K.
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K Conroy
;
K Conroy
*Department of Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, U.K.
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A McQuattie
;
A McQuattie
‡Division of Biochemistry, Department of Chemistry, University of Calgary, Calgary, Alberta, Canada T2N 1N4
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K J Stevenson
K J Stevenson
‡Division of Biochemistry, Department of Chemistry, University of Calgary, Calgary, Alberta, Canada T2N 1N4
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Biochem J (1987) 243 (3): 661–665.
Citation
M J Danson, K Conroy, A McQuattie, K J Stevenson; Dihydrolipoamide dehydrogenase from Trypanosoma brucei. Characterization and cellular location. Biochem J 1 May 1987; 243 (3): 661–665. doi: https://doi.org/10.1042/bj2430661
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