Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1991 Aug;173(16):5144–5150. doi: 10.1128/jb.173.16.5144-5150.1991

L-lyxose metabolism employs the L-rhamnose pathway in mutant cells of Escherichia coli adapted to grow on L-lyxose.

J Badia 1, R Gimenez 1, L Baldomá 1, E Barnes 1, W D Fessner 1, J Aguilar 1
PMCID: PMC208206  PMID: 1650346

Abstract

Escherichia coli cannot grow on L-lyxose, a pentose analog of the 6-deoxyhexose L-rhamnose, which supports the growth of this and other enteric bacteria. L-Rhamnose is metabolized in E. coli by a system that consists of a rhamnose permease, rhamnose isomerase, rhamnulose kinase, and rhamnulose-1-phosphate aldolase, which yields the degradation products dihydroxyacetone phosphate and L-lactaldehyde. This aldehyde is oxidized to L-lactate by lactaldehyde dehydrogenase. All enzymes of the rhamnose system were found to be inducible not only by L-rhamnose but also by L-lyxose. L-Lyxose competed with L-rhamnose for the rhamnose transport system, and purified rhamnose isomerase catalyzed the conversion of L-lyxose into L-xylulose. However, rhamnulose kinase did not phosphorylate L-xylulose sufficiently to support the growth of wild-type E. coli on L-lyxose. Mutants able to grow on L-lyxose were analyzed and found to have a mutated rhamnulose kinase which phosphorylated L-xylulose as efficiently as the wild-type enzyme phosphorylated L-rhamnulose. Thus, the mutated kinase, mapped in the rha locus, enabled the growth of the mutant cells on L-lyxose. The glycolaldehyde generated in the cleavage of L-xylulose 1-phosphate by the rhamnulose-1-phosphate aldolase was oxidized by lactaldehyde dehydrogenase to glycolate, a compound normally utilized by E. coli.

Full text

PDF
5144

Selected References

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

  1. ANDERSON R. L., WOOD W. A. Pathway of L-xylose and L-lyxose degradation in Aerobacter aerogenes. J Biol Chem. 1962 Feb;237:296–303. [PubMed] [Google Scholar]
  2. Bachmann B. J. Linkage map of Escherichia coli K-12, edition 8. Microbiol Rev. 1990 Jun;54(2):130–197. doi: 10.1128/mr.54.2.130-197.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bachmann B. J. Pedigrees of some mutant strains of Escherichia coli K-12. Bacteriol Rev. 1972 Dec;36(4):525–557. doi: 10.1128/br.36.4.525-557.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Badía J., Baldomà L., Aguilar J., Boronat A. Identification of the rhaA, rhaB and rhaD gene products from Escherichia coli K-12. FEMS Microbiol Lett. 1989 Dec;53(3):253–257. doi: 10.1016/0378-1097(89)90226-7. [DOI] [PubMed] [Google Scholar]
  5. 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]
  6. 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]
  7. 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]
  8. Boronat A., Caballero E., Aguilar J. Experimental evolution of a metabolic pathway for ethylene glycol utilization by Escherichia coli. J Bacteriol. 1983 Jan;153(1):134–139. doi: 10.1128/jb.153.1.134-139.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Boulter J. R., Gielow W. O. Properties of D-arabinose isomerase purified from two strains of Escherichia coli. J Bacteriol. 1973 Feb;113(2):687–696. doi: 10.1128/jb.113.2.687-696.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. CHIU T. H., FEINGOLD D. S. THE PURIFICATION AND PROPERTIES OF L-RHAMNULOKINASE. Biochim Biophys Acta. 1964 Dec 23;92:489–497. doi: 10.1016/0926-6569(64)90009-4. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. Chen Y. M., Tobin J. F., Zhu Y., Schleif R. F., Lin E. C. Cross-induction of the L-fucose system by L-rhamnose in Escherichia coli. J Bacteriol. 1987 Aug;169(8):3712–3719. doi: 10.1128/jb.169.8.3712-3719.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. 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]
  15. 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]
  16. DISCHE Z., BORENFREUND E. A new spectrophotometric method for the detection and determination of keto sugars and trioses. J Biol Chem. 1951 Oct;192(2):583–587. [PubMed] [Google Scholar]
  17. Elsinghorst E. A., Mortlock R. P. D-arabinose metabolism in Escherichia coli B: induction and cotransductional mapping of the L-fucose-D-arabinose pathway enzymes. J Bacteriol. 1988 Dec;170(12):5423–5432. doi: 10.1128/jb.170.12.5423-5432.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Fan D. F., Sartoris M., Chiu T. H., Feingold D. S. L-rhamnulose 1-phosphate-1. Methods Enzymol. 1975;41:91–94. doi: 10.1016/s0076-6879(75)41021-7. [DOI] [PubMed] [Google Scholar]
  19. 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]
  20. 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]
  21. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  22. LeBlanc D. J., Mortlock R. P. Metabolism of D-arabinose: a new pathway in Escherichia coli. J Bacteriol. 1971 Apr;106(1):90–96. doi: 10.1128/jb.106.1.90-96.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. 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]
  24. Power J. The L-rhamnose genetic system in Escherichia coli K-12. Genetics. 1967 Mar;55(3):557–568. doi: 10.1093/genetics/55.3.557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. TAKAGI Y., SAWADA H. THE METABOLISM OF L-RHAMNOSE IN ESCHERICHIA COLI. I. L-RHAMNOSE ISOMERASE. Biochim Biophys Acta. 1964 Oct 23;92:10–17. doi: 10.1016/0926-6569(64)90263-9. [DOI] [PubMed] [Google Scholar]
  26. Zhu Y., Lin E. C. An evolvant of Escherichia coli that employs the L-fucose pathway also for growth on L-galactose and D-arabinose. J Mol Evol. 1986;23(3):259–266. doi: 10.1007/BF02115582. [DOI] [PubMed] [Google Scholar]
  27. 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]

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

RESOURCES