Catabolic Pathways for Glucose, Glycerol and 6-Phosphogluconate in Mycobacterium leprae grown in Armadillo Tissues

• Published in: Journal of general microbiology Vol. 129; no. 5; pp. 1481 - 1495
• Main Author: WHEELER, P. R
• Format: Journal Article
• Language: English
• Published: England Soc General Microbiol 01.05.1983
• Subjects: Animals; Armadillos; Electrophoresis, Polyacrylamide Gel; Gluconates - metabolism; Glucose - metabolism; Glycerol - metabolism; Glycolysis; Mycobacterium leprae; Mycobacterium leprae - enzymology; Mycobacterium leprae - metabolism
• ISSN: 0022-1287; 1350-0872; 1465-2080
• DOI: 10.1099/00221287-129-5-1481

National Institute for Medical Research, Mill Hill, London NW7 1AA, U.K. ABSTRACT Summary: With radioisotopes, it was shown that suspensions of Mycobacterium leprae oxidized glycerol, 6-phosphogluconate, glucose, glucose 6-phosphate, and, at a low rate, gluconate, to CO 2 . The incubation period in these experiments was usually 20 h, but after 140 h up to five times more glucose and gluconate had been converted to CO 2 . Studies with differentially labelled glucose indicated that glycolysis and the hexose monophosphate pathway were used for glucose dissimilation. Key enzymes of glycolysis, the hexose monophosphate pathway and glycerol catabolism were detected in cell-free extracts from purified M. leprae, but phosphoketolase, Entner-Doudoroff pathway activity and gluconate kinase were absent. All these enzymes were present also in host-tissue, but biochemical evidence is presented which indicates that all enzymes detected in extracts from M. leprae were authentic bacterial enzymes. Additionally, they could all be detected in extracts of M. leprae prepared by treatment with NaOH in which host enzymes adsorbed to M. leprae are inactivated.