Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1988 Jan;170(1):416–421. doi: 10.1128/jb.170.1.416-421.1988

Metabolism of L-fucose and L-rhamnose in Escherichia coli: aerobic-anaerobic regulation of L-lactaldehyde dissimilation.

L Baldomà 1, J Aguilar 1
PMCID: PMC210658  PMID: 3275622

Abstract

L-Lactaldehyde is a branching point in the metabolic pathway of L-fucose and L-rhamnose utilization. Under aerobic conditions, L-lactaldehyde is oxidized to L-lactate by the enzyme lactaldehyde dehydrogenase, while under anaerobic conditions, L-lactaldehyde is reduced to L-1,2-propanediol by the enzyme propanediol oxidoreductase. Aerobic growth on either of the methyl pentoses induces a lactaldehyde dehydrogenase enzyme which is inhibited by NADH and is very stable under anaerobic conditions. In the absence of oxygen, the cell shifts from the oxidation of L-lactaldehyde to its reduction, owing to both the induction of propanediol oxidoreductase activity and the decrease in the NAD/NADH ratio. The oxidation of L-lactaldehyde to L-lactate is again restored upon a change to aerobic conditions. In this case, only the NAD/NADH ratio may be invoked as a regulatory mechanism, since both enzymes remain active after this change. Experimental evidence in the presence of rhamnose with mutants unable to produce L-lactaldehyde and mutants capable of producing but not further metabolizing it points toward L-lactaldehyde as the effector molecule in the induction of lactaldehyde dehydrogenase. Analysis of a temperature-sensitive mutation affecting the synthesis of lactaldehyde dehydrogenase permitted us to locate an apparently single regulator gene linked to the ald locus at 31 min and probably acting as a positive control element on the expression of the structural gene.

Full text

PDF

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bachmann B. J. Linkage map of Escherichia coli K-12, edition 7. Microbiol Rev. 1983 Jun;47(2):180–230. doi: 10.1128/mr.47.2.180-230.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Baldomà L., Aguilar J. Involvement of lactaldehyde dehydrogenase in several metabolic pathways of Escherichia coli K12. J Biol Chem. 1987 Oct 15;262(29):13991–13996. [PubMed] [Google Scholar]
  3. Boronat A., Aguilar J. Metabolism of L-fucose and L-rhamnose in Escherichia coli: differences in induction of propanediol oxidoreductase. J Bacteriol. 1981 Jul;147(1):181–185. doi: 10.1128/jb.147.1.181-185.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Boronat A., Aguilar J. Rhamnose-induced propanediol oxidoreductase in Escherichia coli: purification, properties, and comparison with the fucose-induced enzyme. J Bacteriol. 1979 Nov;140(2):320–326. doi: 10.1128/jb.140.2.320-326.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Burleigh B. D., Rigby P. W., Hartley B. S. A comparison of wild-type and mutant ribitol dehydrogenases from Klebsiella aerogenes. Biochem J. 1974 Nov;143(2):341–352. doi: 10.1042/bj1430341. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Caballero E., Baldomá L., Ros J., Boronat A., Aguilar J. Identification of lactaldehyde dehydrogenase and glycolaldehyde dehydrogenase as functions of the same protein in Escherichia coli. J Biol Chem. 1983 Jun 25;258(12):7788–7792. [PubMed] [Google Scholar]
  7. Chakrabarti T., Chen Y. M., Lin E. C. Clustering of genes for L-fucose dissimilation by Escherichia coli. J Bacteriol. 1984 Mar;157(3):984–986. doi: 10.1128/jb.157.3.984-986.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Chen Y. M., Lin E. C. Post-transcriptional control of L-1,2-propanediol oxidoreductase in the L-fucose pathway of Escherichia coli K-12. J Bacteriol. 1984 Jan;157(1):341–344. doi: 10.1128/jb.157.1.341-344.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. 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]
  11. Chiu T. H., Feingold D. S. L-rhamnulose 1-phosphate aldolase from Escherichia coli. Crystallization and properties. Biochemistry. 1969 Jan;8(1):98–108. doi: 10.1021/bi00829a015. [DOI] [PubMed] [Google Scholar]
  12. Cocks G. T., Aguilar T., Lin E. C. Evolution of L-1, 2-propanediol catabolism in Escherichia coli by recruitment of enzymes for L-fucose and L-lactate metabolism. J Bacteriol. 1974 Apr;118(1):83–88. doi: 10.1128/jb.118.1.83-88.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. GHALAMBOR M. A., HEATH E. C. The metabolism of L-fucose. II. The enzymatic cleavage of L-fuculose 1-phosphate. J Biol Chem. 1962 Aug;237:2427–2433. [PubMed] [Google Scholar]
  14. GREEN M., COHEN S. S. Enzymatic conversion of L-fucose to L-fuculose. J Biol Chem. 1956 Apr;219(2):557–568. [PubMed] [Google Scholar]
  15. HEATH E. C., GHALAMBOR M. A. The metabolism of L-fucose. I. The purification and properties of L-fuculose kinase. J Biol Chem. 1962 Aug;237:2423–2426. [PubMed] [Google Scholar]
  16. 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]
  17. Hacking A. J., Lin E. C. Disruption of the fucose pathway as a consequence of genetic adaptation to propanediol as a carbon source in Escherichia coli. J Bacteriol. 1976 Jun;126(3):1166–1172. doi: 10.1128/jb.126.3.1166-1172.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Keleti T., Welch G. R. The evolution of enzyme kinetic power. Biochem J. 1984 Oct 15;223(2):299–303. doi: 10.1042/bj2230299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. 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]
  20. Laurell C. B. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal Biochem. 1966 Apr;15(1):45–52. doi: 10.1016/0003-2697(66)90246-6. [DOI] [PubMed] [Google Scholar]
  21. Lin E. C. Glycerol dissimilation and its regulation in bacteria. Annu Rev Microbiol. 1976;30:535–578. doi: 10.1146/annurev.mi.30.100176.002535. [DOI] [PubMed] [Google Scholar]
  22. 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]
  23. Sridhara S., Wu T. T. Purification and properties of lactaldehyde dehydrogenase from Escherichia coli. J Biol Chem. 1969 Oct 10;244(19):5233–5238. [PubMed] [Google Scholar]
  24. TAKAGI Y., SAWADA H. THE METABOLISM OF L-RHAMNOSE IN ESCHERICHIA COLI. II. L-RHAMNULOSE KINASE. Biochim Biophys Acta. 1964 Oct 23;92:18–25. doi: 10.1016/0926-6569(64)90264-0. [DOI] [PubMed] [Google Scholar]
  25. Wimpenny J. W., Firth A. Levels of nicotinamide adenine dinucleotide and reduced nicotinamide adenine dinucleotide in facultative bacteria and the effect of oxygen. J Bacteriol. 1972 Jul;111(1):24–32. doi: 10.1128/jb.111.1.24-32.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Wright J. A., Sanwal B. D. Regulatory mechanisms involving nicotinamide adenine nucleotides as all teric effectors. II. Control of phosphoenolpyruvate carboxykinase. J Biol Chem. 1969 Apr 10;244(7):1838–1845. [PubMed] [Google Scholar]
  27. de Bruijn F. J., Lupski J. R. The use of transposon Tn5 mutagenesis in the rapid generation of correlated physical and genetic maps of DNA segments cloned into multicopy plasmids--a review. Gene. 1984 Feb;27(2):131–149. doi: 10.1016/0378-1119(84)90135-5. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES