Abstract
When resting cells of Neisseria meningitidis group B were incubated with either succinate, fumarate, or malate, respiration and CO2 production were not significantly stimulated. These dicarboxylic acids were readily utilized, however, when they were added in association with a combination of α-ketoglutarate and aspartate or with glucose or with glutamate. The amounts of these substrates required for exogenous succinate utilization were relatively large. Both the α-ketoglutarate–aspartate combination and glutamate greatly stimulated succinate uptake into the cells, but glutamate was far more effective than the α-ketoglutarate–aspartate combination in eliciting exogenous succinate utilization. This difference is explained on the basis of evidence reported in another article that succinate derived from the α-ketoglutarate-aspartate mixture is metabolized more rapidly—and thus more rapidly dilutes the specific activity of added succinate—than the succinate derived from glutamate.
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- BOVARNICK M. R., SCHNEIDER L. The incorporation of glycine-1-C14 by typhus rickettsiae. J Biol Chem. 1960 Jun;235:1727–1731. [PubMed] [Google Scholar]
- CAMPBELL J. J. R., STOKES F. N. Tricarboxylic acid cycle in Pseudomonas aeruginosa. J Biol Chem. 1951 Jun;190(2):853–858. [PubMed] [Google Scholar]
- CLARKE P. H., MEADOW P. M. Evidence for the occurrence of Permeases for tricarboxylic acid cycle intermediates in Pseudomonas aeruginosa. J Gen Microbiol. 1959 Feb;20(1):144–155. doi: 10.1099/00221287-20-1-144. [DOI] [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]
- HALPERN Y. S., EVEN-SHOSHAN A., ARTMAN M. EFFECT OF GLUCOSE ON THE UTILIZATION OF SUCCINATE AND THE ACTIVITY OF TRICARBOXYLIC ACID-CYCLE ENZYMES IN ESCHERICHIA COLI. Biochim Biophys Acta. 1964 Nov 8;93:228–236. doi: 10.1016/0304-4165(64)90370-8. [DOI] [PubMed] [Google Scholar]
- Heppel L. A. Selective release of enzymes from bacteria. Science. 1967 Jun 16;156(3781):1451–1455. doi: 10.1126/science.156.3781.1451. [DOI] [PubMed] [Google Scholar]
- KOGUT M., PODOSKI E. P. Oxidative pathways in a fluorescent Pseudomonas. Biochem J. 1953 Dec;55(5):800–811. doi: 10.1042/bj0550800. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MACQUILLAN A. M., HALVORSON H. O. Physiological changes occurring in yeast undergoing glucose repression. J Bacteriol. 1962 Jul;84:31–36. doi: 10.1128/jb.84.1.31-36.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mallavia L. P., Weiss E. Catabolic activities of Neisseria meningitidis: utilization of glutamate. J Bacteriol. 1970 Jan;101(1):127–132. doi: 10.1128/jb.101.1.127-132.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- REPASKE R., SHROAT J., ALLMAN D. Permeability of Azotobacter to succinate and malate. J Bacteriol. 1960 Mar;79:394–405. doi: 10.1128/jb.79.3.394-405.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]