Abstract
Washed-cell preparations of Mycobacterium tuberculosis strain H37Ra and M. smegmatis 607 grown in Sauton's medium demonstrated a lag in glutamate oxidation. Washed-cell preparations of M. fortuitum and M. phlei oxidized glutamate immediately and in a linear fashion. Glutamate was oxidized without a lag by washed cells of M. tuberculosis H37Ra and M. smegmatis 607 harvested from a modified medium containing glutamate. Chloramphenicol inhibited the oxidation of glutamate by washed cells grown in the absence of glutamate. These findings suggested the induction of either an enzyme system for glutamate oxidation or a glutamate transport system. The activity of glutamic dehydrogenase was not significantly greater in extracts prepared from cells grown with glutamate. However, the initial rate of glutamate uptake by induced cells was three to four times higher than in noninduced cells. The induction of the glutamate transport system in M. tuberculosis H37Ra and M. smegmatis 607 was shown to parallel the induction of glutamate oxidation. After a 60-min lag, the inducible glutamate transport system appeared. Chloramphenicol prevented the induction of glutamate uptake, although the antibiotic had no effect on glutamate uptake by previously induced cells. Some of the properties of this glutamate uptake system are described.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- AMES G. F. UPTAKE OF AMINO ACIDS BY SALMONELLA TYPHIMURIUM. Arch Biochem Biophys. 1964 Jan;104:1–18. doi: 10.1016/s0003-9861(64)80028-x. [DOI] [PubMed] [Google Scholar]
- BRITTEN R. J., McCLURE F. T. The amino acid pool in Escherichia coli. Bacteriol Rev. 1962 Sep;26:292–335. doi: 10.1128/br.26.3.292-335.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
- COHEN G. N., MONOD J. Bacterial permeases. Bacteriol Rev. 1957 Sep;21(3):169–194. doi: 10.1128/br.21.3.169-194.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
- EDSON N. L. The intermediary metabolism of the mycobacteria. Bacteriol Rev. 1951 Sep;15(3):147–182. doi: 10.1128/br.15.3.147-182.1951. [DOI] [PMC free article] [PubMed] [Google Scholar]
- ELLARD G. A., CLARKE P. H. Acetate and fumarate permeases of Mycobacterium smegmatis. J Gen Microbiol. 1959 Oct;21:338–343. doi: 10.1099/00221287-21-2-338. [DOI] [PubMed] [Google Scholar]
- HALPERN Y. S., UMBARGER H. E. Conversion of ammonia to amino groups in Escherichia coli. J Bacteriol. 1960 Sep;80:285–288. doi: 10.1128/jb.80.3.285-288.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LYON R. H., LICHSTEIN H. C., HALL W. H. Influence of age on metabolic activity of Mycobacterium tuberculosis. Proc Soc Exp Biol Med. 1958 Oct;99(1):79–81. doi: 10.3181/00379727-99-24253. [DOI] [PubMed] [Google Scholar]
- MURTHY P. S., SIRSI M., RAMAKRISHNAN T. Tricarboxylic acid cycle and related enzymes in cell-free extracts of Mycobacterium tuberculosis H37Rv. Biochem J. 1962 Aug;84:263–269. doi: 10.1042/bj0840263. [DOI] [PMC free article] [PubMed] [Google Scholar]
- OTT J. L. Asparaginase from mycobacteria. J Bacteriol. 1960 Sep;80:355–361. doi: 10.1128/jb.80.3.355-361.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
- YOUMANS A. S., MILLMAN I., YOUMANS G. P. The oxidation of compounds related to the tricarboxylic acid cycle by whole cells and enzyme preparations of Mycobacterium tuberculosis var. hominis. J Bacteriol. 1956 May;71(5):565–570. doi: 10.1128/jb.71.5.565-570.1956. [DOI] [PMC free article] [PubMed] [Google Scholar]