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. 1989 Feb;171(2):862–867. doi: 10.1128/jb.171.2.862-867.1989

L-1,2-propanediol exits more rapidly than L-lactaldehyde from Escherichia coli.

Y Zhu 1, E C Lin 1
PMCID: PMC209675  PMID: 2644239

Abstract

Catabolism of the six-carbon compound L-fucose results in formation of dihydroxyacetone phosphate (C-1-to-C-3 fragment) and L-lactaldehyde (C-4-to-C-6 fragment) as intermediates. The fate of lactaldehyde depends on the respiratory growth conditions. Aerobically, lactaldehyde is oxidized to L-lactate by an NAD-linked dehydrogenase (ald product). L-Lactate, in turn, is converted to pyruvate, which enters the general metabolic pool. Anaerobically, lactaldehyde is reduced to L-1,2-propanediol by an NADH-linked oxidoreductase (fucO product). L-1,2-Propanediol is excreted as a terminal fermentation product. In a previous study, we showed that retention of the C-4-to-C-6 fragment of fucose depended on the competition for lactaldehyde by aldehyde dehydrogenase and propanediol oxidoreductase (Y. Zhu and E.C.C. Lin, J. Bacteriol. 169:785-789, 1987). In this study, we compared the wild-type strain and isogenic mutant strains defective in ald, fucO, or both for ability to accumulate radioactivity when incubated with fucose labeled at either the C-1 or the C-6 position. The results showed that although blocking the oxidation of lactaldehyde prevented its assimilation, rapid exit of the 3-carbon unit occurred only when the compound was reduced to propanediol. Moreover, growth experiments on fucose indicated that a double ald fucO mutant accumulated inhibiting concentrations of lactaldehyde. The inner cell membrane therefore appears to be much more permeable to the 3-carbon alcohol than to the 3-carbon aldehyde. The almost instantaneous exit of propanediol appears to be a facilitated process.

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Selected References

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  1. Baldoma L., Badia J., Obradors N., Aguilar J. Aerobic excretion of 1,2-propanediol by Salmonella typhimurium. J Bacteriol. 1988 Jun;170(6):2884–2885. doi: 10.1128/jb.170.6.2884-2885.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Chen Y. M., Lin E. C., Ros J., Aguilar J. Use of operon fusions to examine the regulation of the L-1,2-propanediol oxidoreductase gene of the fucose system in Escherichia coli K12. J Gen Microbiol. 1983 Nov;129(11):3355–3362. doi: 10.1099/00221287-129-11-3355. [DOI] [PubMed] [Google Scholar]
  3. Chen Y. M., Zhu Y., Lin E. C. NAD-linked aldehyde dehydrogenase for aerobic utilization of L-fucose and L-rhamnose by Escherichia coli. J Bacteriol. 1987 Jul;169(7):3289–3294. doi: 10.1128/jb.169.7.3289-3294.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hacking A. J., Aguilar J., Lin E. C. Evolution of propanediol utilization in Escherichia coli: mutant with improved substrate-scavenging power. J Bacteriol. 1978 Nov;136(2):522–530. doi: 10.1128/jb.136.2.522-530.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Heller K. B., Lin E. C., Wilson T. H. Substrate specificity and transport properties of the glycerol facilitator of Escherichia coli. J Bacteriol. 1980 Oct;144(1):274–278. doi: 10.1128/jb.144.1.274-278.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. Novotny M. J., Frederickson W. L., Waygood E. B., Saier M. H., Jr Allosteric regulation of glycerol kinase by enzyme IIIglc of the phosphotransferase system in Escherichia coli and Salmonella typhimurium. J Bacteriol. 1985 May;162(2):810–816. doi: 10.1128/jb.162.2.810-816.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Postma P. W., Epstein W., Schuitema A. R., Nelson S. O. Interaction between IIIGlc of the phosphoenolpyruvate:sugar phosphotransferase system and glycerol kinase of Salmonella typhimurium. J Bacteriol. 1984 Apr;158(1):351–353. doi: 10.1128/jb.158.1.351-353.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Richey D. P., Lin E. C. Importance of facilitated diffusion for effective utilization of glycerol by Escherichia coli. J Bacteriol. 1972 Nov;112(2):784–790. doi: 10.1128/jb.112.2.784-790.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Sanno Y., Wilson T. H., Lin E. C. Control of permeation to glycerol in cells of Escherichia coli. Biochem Biophys Res Commun. 1968 Jul 26;32(2):344–349. doi: 10.1016/0006-291x(68)90392-6. [DOI] [PubMed] [Google Scholar]
  11. Sridhara S., Wu T. T., Chused T. M., Lin E. C. Ferrous-activated nicotinamide adenine dinucleotide-linked dehydrogenase from a mutant of Escherichia coli capable of growth on 1, 2-propanediol. J Bacteriol. 1969 Apr;98(1):87–95. doi: 10.1128/jb.98.1.87-95.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Zagalak B., Frey P. A., Karabatsos G. L., Abeles R. H. The stereochemistry of the conversion of D and L 1,2-propanediols to propionaldehyde. J Biol Chem. 1966 Jul 10;241(13):3028–3035. [PubMed] [Google Scholar]
  13. Zhu Y., Lin E. C. A mutant crp allele that differentially activates the operons of the fuc regulon in Escherichia coli. J Bacteriol. 1988 May;170(5):2352–2358. doi: 10.1128/jb.170.5.2352-2358.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Zhu Y., Lin E. C. Loss of aldehyde dehydrogenase in an Escherichia coli mutant selected for growth on the rare sugar L-galactose. J Bacteriol. 1987 Feb;169(2):785–789. doi: 10.1128/jb.169.2.785-789.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Zwaig N., Kistler W. S., Lin E. C. Glycerol kinase, the pacemaker for the dissimilation of glycerol in Escherichia coli. J Bacteriol. 1970 Jun;102(3):753–759. doi: 10.1128/jb.102.3.753-759.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. de Boer M., Broekhuizen C. P., Postma P. W. Regulation of glycerol kinase by enzyme IIIGlc of the phosphoenolpyruvate:carbohydrate phosphotransferase system. J Bacteriol. 1986 Jul;167(1):393–395. doi: 10.1128/jb.167.1.393-395.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]

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