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Gene Review:

Tb09.160.4380 - succinate dehydrogenase

Trypanosoma brucei brucei TREU927

Opperdoes, F.R. et al., Beattie, D.S. et al., van Weelden, S.W. et al., Bochud-Allemann, N. et al., Turrens, J.F.

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High impact information on Tb09.160.4380

We also demonstrate that the subsequent enzymes of the Krebs cycle, succinate dehydrogenase and fumarase, are most likely used for conversion of succinate into malate, which can then be used in gluconeogenesis [1].
2) Succinate dehydrogenase appears to be the only entry point for electrons of mitochondrial substrates into the respiratory chain; however, its activity could be ablated without causing a growth phenotype [2].
Addition of malonate, an inhibitor of succinate dehydrogenase, stimulated NAD(P)H reduction [3].
The presence of an alternative pathway for NADH oxidation involving fumarate reductase was indicated by the observation that malonate, the specific inhibitor of succinate dehydrogenase, inhibited 30-35% the rate of oxygen uptake with malate and glucose as substrates in the digitonin-permeabilized cells [4].
Succinate dehydrogenase and sn-glycerol-3-phosphate dehydrogenase, together with oligomycin-sensitive ATPase, were located in the mitochondrion which had a density in sucrose ranging from 1.16 to 1.18 g/cm3 [5].

References

New functions for parts of the Krebs cycle in procyclic Trypanosoma brucei, a cycle not operating as a cycle. van Weelden, S.W., van Hellemond, J.J., Opperdoes, F.R., Tielens, A.G. J. Biol. Chem. (2005) [Pubmed]
Mitochondrial substrate level phosphorylation is essential for growth of procyclic Trypanosoma brucei. Bochud-Allemann, N., Schneider, A. J. Biol. Chem. (2002) [Pubmed]
The role of succinate in the respiratory chain of Trypanosoma brucei procyclic trypomastigotes. Turrens, J.F. Biochem. J. (1989) [Pubmed]
Oxidation of NADH by a rotenone and antimycin-sensitive pathway in the mitochondrion of procyclic Trypanosoma brucei brucei. Beattie, D.S., Obungu, V.H., Kiaira, J.K. Mol. Biochem. Parasitol. (1994) [Pubmed]
Localization of malate dehydrogenase, adenylate kinase and glycolytic enzymes in glycosomes and the threonine pathway in the mitochondrion of cultured procyclic trypomastigotes of Trypanosoma brucei. Opperdoes, F.R., Markoŝ, A., Steiger, R.F. Mol. Biochem. Parasitol. (1981) [Pubmed]

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