Oxidation of carbon sources through the tricarboxylic acid cycle in Mycobacterium leprae grown in armadillo liver.
All the enzymes of the tricarboxylic acid cycle have now been demonstrated in extracts of Mycobacterium leprae grown in armadillo liver. Many were also present in homogenates of host-tissue, but biochemical evidence is presented which indicates that all enzymes detected in extracts from M. leprae were authentic bacterial enzymes. Further evidence for a complete tricarboxylic acid cycle in M. leprae was obtained by first establishing that citrate could be taken up and catabolized by whole M. leprae organisms, then showing that oxidation of radioisotopically labelled pyruvate to CO2 by suspensions of M. leprae was stimulated by adding unlabelled citrate. Control of tricarboxylic acid cycle activity in M. leprae by the inactivation of fumarase by a protease is speculated upon.
D000818:Animals; D001135:Armadillos; D002952:Citric Acid Cycle; D004591:Electrophoresis, Polyacrylamide Gel; D007521:Isocitrate Dehydrogenase / Q000378:metabolism; D008099:Liver / Q000201:enzymology / Q000382:microbiology*; D009166:Mycobacterium leprae / Q000201:enzymology / Q000378:metabolism*; D011768:Pyruvate Dehydrogenase Complex / Q000378:metabolism; D013385:Succinate Dehydrogenase / Q000378:metabolism
D011768:Pyruvate Dehydrogenase Complex; D007521:Isocitrate Dehydrogenase; D013385:Succinate Dehydrogenase