Abstract
The growth of an anaerobic, spore-forming rod we have isolated from the cockroach gut after enrichment on media containing PPi was stimulated by the presence of PPi. The doubling time decreased and cell yield increased proportionately to PPi concentrations of up to 0.35%. A similar stimulation of the growth of Desulfotomaculum sp. by PPi has been reported. The PPi-stimulated Clostridium sp. fermented a number of sugars with the production of hydrogen, acetate, and butyrate, with smaller amounts of ethanol and butanol being produced from some substrates. The fermentation products were not qualitatively changed by the presence of PPi, but significantly more hydrogen was produced. The organism contained several of the enzymes previously reported from Entamoeba sp. and Propionibacterium sp., in which PPi serves as a source of a high-energy bond in place of ATP. These include significant amounts of pyruvate-phosphate dikinase and phosphoenolpyruvate carboxytransphosphorylase. The activities of many of the catabolic enzymes of the organism, as well as of its phosphatases and pyrophosphatase, were similar whether it was grown in the presence or absence of PPi. The organism did not accumulate intracellular polyphosphate granules but stored large amounts of glycogen.
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- Cruden D. L., Gorrell T. E., Markovetz A. J. Novel microbial and chemical components of a specific black-band region in the cockroach hindgut. J Bacteriol. 1979 Nov;140(2):687–698. doi: 10.1128/jb.140.2.687-698.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dassa E., Boquet P. L. Is the acid phosphatase of Escherichia coli with pH optimum of 2.5 A polyphosphate depolymerase? FEBS Lett. 1981 Nov 30;135(1):148–150. doi: 10.1016/0014-5793(81)80964-7. [DOI] [PubMed] [Google Scholar]
- Dawes E. A., Senior P. J. The role and regulation of energy reserve polymers in micro-organisms. Adv Microb Physiol. 1973;10:135–266. doi: 10.1016/s0065-2911(08)60088-0. [DOI] [PubMed] [Google Scholar]
- Forsberg C. W., Cheng K. J. The constitutive nature of alkaline phosphatase in rumen bacteria. Can J Microbiol. 1980 Feb;26(2):268–272. doi: 10.1139/m80-043. [DOI] [PubMed] [Google Scholar]
- Harold F. M. Inorganic polyphosphates in biology: structure, metabolism, and function. Bacteriol Rev. 1966 Dec;30(4):772–794. doi: 10.1128/br.30.4.772-794.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Harwood C. S., Canale-Parola E. Properties of acetate kinase isozymes and a branched-chain fatty acid kinase from a spirochete. J Bacteriol. 1982 Oct;152(1):246–254. doi: 10.1128/jb.152.1.246-254.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KELLENBERGER E., RYTER A., SECHAUD J. Electron microscope study of DNA-containing plasms. II. Vegetative and mature phage DNA as compared with normal bacterial nucleoids in different physiological states. J Biophys Biochem Cytol. 1958 Nov 25;4(6):671–678. doi: 10.1083/jcb.4.6.671. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Laanbroek H. J., Pfennig N. Oxidation of short-chain fatty acids by sulfate-reducing bacteria in freshwater and in marine sediments. Arch Microbiol. 1981 Jan;128(3):330–335. doi: 10.1007/BF00422540. [DOI] [PubMed] [Google Scholar]
- Liu C. L., Hart N., Peck H. D., Jr Inorganic pyrophosphate: energy source for sulfate-reducing bacteria of the genus desulfotomaculum. Science. 1982 Jul 23;217(4557):363–364. doi: 10.1126/science.217.4557.363. [DOI] [PubMed] [Google Scholar]
- Liu C. L., Peck H. D., Jr Comparative bioenergetics of sulfate reduction in Desulfovibrio and Desulfotomaculum spp. J Bacteriol. 1981 Feb;145(2):966–973. doi: 10.1128/jb.145.2.966-973.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- O'Brien W. E., Bowien S., Wood H. G. Isolation and characterization of a pyrophosphate-dependent phosphofructokinase from Propionibacterium shermanii. J Biol Chem. 1975 Nov 25;250(22):8690–8695. [PubMed] [Google Scholar]
- Potrikus C. J., Breznak J. A. Nitrogen-fixing Enterobacter agglomerans isolated from guts of wood-eating termites. Appl Environ Microbiol. 1977 Feb;33(2):392–399. doi: 10.1128/aem.33.2.392-399.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Reeves R. E. A new enzyme with the glycolytic function of pyruvate kinase. J Biol Chem. 1968 Jun 10;243(11):3202–3204. [PubMed] [Google Scholar]
- Reeves R. E., Guthrie J. D. Acetate kinase (pyrophosphate). A fourth pyrophosphate-dependent kinase from Entamoeba histolytica. Biochem Biophys Res Commun. 1975 Oct 27;66(4):1389–1395. doi: 10.1016/0006-291x(75)90513-6. [DOI] [PubMed] [Google Scholar]
- Reeves R. E., Menzies R. A., Hsu D. S. The pyruvate-phosphate dikinase reaction. The fate of phosphate and the equilibrium. J Biol Chem. 1968 Oct 25;243(20):5486–5491. [PubMed] [Google Scholar]
- Roberton A. M., Glucina P. G. Fructose 6-phosphate phosphorylation in Bacteroides species. J Bacteriol. 1982 Jun;150(3):1056–1060. doi: 10.1128/jb.150.3.1056-1060.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sawyer M. H., Baumann P., Baumann L. Pathways of D-fructose and D-glucose catabolism in marine species of Alcaligenes, Pseudomonas marina, and Alteromonas communis. Arch Microbiol. 1977 Mar 1;112(2):169–172. doi: 10.1007/BF00429331. [DOI] [PubMed] [Google Scholar]
- Wood H. G., O'brien W. E., Micheales G. Properties of carboxytransphosphorylase; pyruvate, phosphate dikinase; pyrophosphate-phosphofructikinase and pyrophosphate-acetate kinase and their roles in the metabolism of inorganic pyrophosphate. Adv Enzymol Relat Areas Mol Biol. 1977;45:85–155. doi: 10.1002/9780470122907.ch2. [DOI] [PubMed] [Google Scholar]

