Metabolism in Mycobacterium leprae: its relation to other research on M. leprae and to aspects of metabolism in other mycobacteria and intracellular parasites.
Recently, some knowledge of metabolic pathways, rather than individual enzyme activities of M. leprae, is becoming available. Ultimately this may be useful in devising culture media for M. leprae. Knowledge restricted to individual reactions may be misleading. For instance, the detection of GlcNacase and beta-glucuronidase and the subcellular localization of hyaluronic acid led to attempts to cultivate M. leprae on hyaluronic-acid based medium. Subsequent investigations suggested that there was no pathway for the breakdown of hyaluronic acid in M. leprae. The biochemical pathways for breaking down glucose and glycerol seem to be complete, and thus similar to many bacteria, but there is an unusually high level of one enzyme, 6-phosphogluconate dehydrogenase (6PGDH). Although 6-phosphogluconate is oxidized by M. leprae, and this is an unusual activity, reflecting very high levels of 6PGDH, glycerol may be a preferable energy source (on the basis of rates of oxidation by suspensions) for M. leprae in attempts to cultivate the bacterium. The utilization of 6-phosphogluconate might be important for other aspects of M. leprae metabolism not yet investigated (e.g., pentose metabolism) or it may be an adaption, not needed in vitro, to its existence in host macrophages. Alternatively, its oxidation may be a way of rapidly generating NADPH at critical times for the bacterium. Other unusual activities which have been reported are the presence of an enzyme characteristic of chemoautotrophism , completely surprising in view of the biology of M. leprae. This report needs to be confirmed--some aspects, in fact, have failed to be confirmed. o-Diphenoloxidase activity is unique, among mycobacteria, to M. leprae, but there is still doubt over whether or not it is an enzymatic activity and its function is unknown. A transpeptidase which may be involved in cell wall synthesis, recently demonstrated in M. leprae, is a typical mycobacterial enzyme. It is now known that iron could be supplied to M. leprae in potential media in the form of ferriexochelin from M. neoaurum . Two "deletions" in the metabolic processes of M. leprae have been observed. Catalase appears to be absent in M. leprae; its addition to media stimulates the growth of some organisms since peroxides form in the bacteriological media . Purine synthesis de novo occurred at a very low rate compared with purine scavenging. Whether this is an adaption to growth in vivo is not known.(ABSTRACT TRUNCATED AT 400 WORDS)
D000118:Acetylglucosaminidase / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000596:Amino Acids / Q000378:metabolism; D001431:Bacteriological Techniques; D002374:Catalase / Q000378:metabolism; D003470:Culture Media; D004269:DNA, Bacterial / Q000302:isolation & purification; D004295:Dihydroxyphenylalanine / Q000302:isolation & purification; D004579:Electron Transport; D005609:Free Radicals; D005942:Gluconates / Q000378:metabolism; D005947:Glucose / Q000378:metabolism; D005966:Glucuronidase / Q000378:metabolism; D007527:Isoenzymes / Q000378:metabolism; D009166:Mycobacterium leprae / Q000254:growth & development / Q000378:metabolism*; D009696:Nucleic Acids / Q000378:metabolism; D010085:Oxidative Phosphorylation; D009195:Peroxidase; D010544:Peroxidases / Q000378:metabolism; D005723:gamma-Glutamyltransferase / Q000378:metabolism
D000596:Amino Acids; D003470:Culture Media; D004269:DNA, Bacterial; D005609:Free Radicals; D005942:Gluconates; D007527:Isoenzymes; D009696:Nucleic Acids; D004295:Dihydroxyphenylalanine; D000255:Adenosine Triphosphate; D010544:Peroxidases; D002374:Catalase; D009195:Peroxidase; D005723:gamma-Glutamyltransferase; D005966:Glucuronidase; D000118:Acetylglucosaminidase; D005947:Glucose; C030691:gluconic acid; C008884:6-phosphogluconic acid