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. 1968 Feb;106(4):847–858. doi: 10.1042/bj1060847

Control of amino sugar metabolism in Escherichia coli and isolation of mutants unable to degrade amino sugars

R J White 1
PMCID: PMC1198589  PMID: 4866432

Abstract

1. Growth of Escherichia coli on glucosamine results in an induction of glucosamine 6-phosphate deaminase [2-amino-2-deoxy-d-glucose 6-phosphate ketol-isomerase (deaminating), EC 5.3.1.10] and a repression of glucosamine 6-phosphate synthetase (l-glutamine–d-fructose 6-phosphate aminotransferase, EC 2.6.1.16); glucose abolishes these control effects. 2. Growth of E. coli on N-acetylglucosamine results in an induction of N-acetylglucosamine 6-phosphate deacetylase and glucosamine 6-phosphate deaminase, and in a repression of glucosamine 6-phosphate synthetase; glucose diminishes these control effects. 3. The synthesis of amino sugar kinases (EC 2.7.1.8 and 2.7.1.9) is unaffected by growth on amino sugars. 4. Glucosamine 6-phosphate synthetase is inhibited by glucosamine 6-phosphate. 5. Mutants of E. coli that are unable to grow on N-acetylglucosamine have been isolated, and lack either N-acetylglucosamine 6-phosphate deacetylase (deacetylaseless) or glucosamine 6-phosphate deaminase (deaminaseless). Deacetylaseless mutants can grow on glucosamine but deaminaseless mutants cannot. 6. After growth on glucose, deacetylaseless mutants have a repressed glucosamine 6-phosphate synthetase and a super-induced glucosamine 6-phosphate deaminase; this may be related to an intracellular accumulation of acetylamino sugar that also occurs under these conditions. In one mutant the acetylamino sugar was shown to be partly as N-acetylglucosamine 6-phosphate. Deaminaseless mutants have no abnormal control effects after growth on glucose. 7. Addition of N-acetylglucosamine or glucosamine to cultures of a deaminaseless mutant caused inhibition of growth. Addition of N-acetylglucosamine to cultures of a deacetylaseless mutant caused lysis, and secondary mutants were isolated that did not lyse; most of these secondary mutants had lost glucosamine 6-phosphate deaminase and an uptake mechanism for N-acetylglucosamine. 8. Similar amounts of 14C were incorporated from [1-14C]-glucosamine by cells of mutants and wild-type growing on broth. Cells of wild-type and a deaminaseless mutant incorporated 14C from N-acetyl[1-14C]glucosamine more efficiently than from N[1-14C]-acetylglucosamine, incorporation from the latter being further decreased by acetate; cells of a deacetylaseless mutant showed a poor incorporation of both types of labelled N-acetylglucosamine.

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Selected References

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

  1. BATES C. J., PASTERNAK C. A. FURTHER STUDIES ON THE REGULATION OF AMINO SUGAR METABOLISM IN BACILLUS SUBTILIS. Biochem J. 1965 Jul;96:147–154. doi: 10.1042/bj0960147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BATES C. J., PASTERNAK C. A. THE INCORPORATION OF LABELLED AMINO SUGARS BY BACILLUS SUBTILIS. Biochem J. 1965 Jul;96:155–158. doi: 10.1042/bj0960155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. CLARKE J. S., PASTERNAK C. A. The regulation of amino sugar metabolism in Bacillus subtilis. Biochem J. 1962 Jul;84:185–191. doi: 10.1042/bj0840185. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. COMB D. G., ROSEMAN S. Glucosamine metabolism. IV. Glucosamine-6-phosphate deaminase. J Biol Chem. 1958 Jun;232(2):807–827. [PubMed] [Google Scholar]
  5. DAVIS B. D., MINGIOLI E. S. Mutants of Escherichia coli requiring methionine or vitamin B12. J Bacteriol. 1950 Jul;60(1):17–28. doi: 10.1128/jb.60.1.17-28.1950. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. DORFMAN A. Metabolism of the mucopolysaccharides of connective tissue. Pharmacol Rev. 1955 Mar;7(1):1–31. [PubMed] [Google Scholar]
  7. FUKASAWA T., NIKAIDO H. Galactose-sensitive mutants of Salmonella. II. Bacteriolysis induced by galactose. Biochim Biophys Acta. 1961 Apr 15;48:470–483. doi: 10.1016/0006-3002(61)90045-2. [DOI] [PubMed] [Google Scholar]
  8. INGRAM V. M., SALTON M. R. The action of fluorodinitrobenzene on bacterial cell walls. Biochim Biophys Acta. 1957 Apr;24(1):9–14. doi: 10.1016/0006-3002(57)90139-7. [DOI] [PubMed] [Google Scholar]
  9. KORNFELD S., GLASER L. The synthesis of thymidine-linked sugars. v. thymidine diphosphate-amino sugars. J Biol Chem. 1962 Oct;237:3052–3059. [PubMed] [Google Scholar]
  10. KORNFELD S., KORNFELD R., NEUFELD E. F., O'BRIEN P. J. THE FEEDBACK CONTROL OF SUGAR NUCLEOTIDE BIOSYNTHESIS IN LIVER. Proc Natl Acad Sci U S A. 1964 Aug;52:371–379. doi: 10.1073/pnas.52.2.371. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. KUNDIG W., GHOSH S., ROSEMAN S. PHOSPHATE BOUND TO HISTIDINE IN A PROTEIN AS AN INTERMEDIATE IN A NOVEL PHOSPHO-TRANSFERASE SYSTEM. Proc Natl Acad Sci U S A. 1964 Oct;52:1067–1074. doi: 10.1073/pnas.52.4.1067. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. LAMBERT R., SAITO Y., VEERKAMP J. H. INCORPORATION OF LABELED DERIVATIVES OF 2-DEOXY-2-AMINO-D-GLUCOSE INTO THE CELL WALLS OF LACTOBACILLUS BIFIDUS VAR. PENNSYLVANICUS. Arch Biochem Biophys. 1965 May;110:341–345. doi: 10.1016/0003-9861(65)90130-x. [DOI] [PubMed] [Google Scholar]
  13. LEVVY G. A., MCALLAN A. The N-acetylation and estimation of hexosamines. Biochem J. 1959 Sep;73:127–132. doi: 10.1042/bj0730127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Loomis W. F., Jr, Magasanik B. Glucose-lactose diauxie in Escherichia coli. J Bacteriol. 1967 Apr;93(4):1397–1401. doi: 10.1128/jb.93.4.1397-1401.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. MAGASANIK B. Catabolite repression. Cold Spring Harb Symp Quant Biol. 1961;26:249–256. doi: 10.1101/sqb.1961.026.01.031. [DOI] [PubMed] [Google Scholar]
  16. NAKADA H. I., WOLFE J. B. Glucosamine degradation by Escherichia coli. II. The isomeric conversion of glucosamine 6-PO4 to fructose 6-PO4 and ammonia. Arch Biochem Biophys. 1956 Oct;64(2):489–497. doi: 10.1016/0003-9861(56)90291-0. [DOI] [PubMed] [Google Scholar]
  17. Partridge S. M. Filter-paper partition chromatography of sugars: 1. General description and application to the qualitative analysis of sugars in apple juice, egg white and foetal blood of sheep. with a note by R. G. Westall. Biochem J. 1948;42(2):238–250. doi: 10.1042/bj0420238. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. ROSEMAN S. Glucosamine metabolism. I. N-acetylglucosamine deacetylase. J Biol Chem. 1957 May;226(1):115–124. [PubMed] [Google Scholar]
  19. Schlesinger S., Scotto P., Magasanik B. Exogenous and endogenous induction of the histidine-degrading enzymes in Aerobacter aerogenes. J Biol Chem. 1965 Nov;240(11):4331–4337. [PubMed] [Google Scholar]
  20. TREVELYAN W. E., PROCTER D. P., HARRISON J. S. Detection of sugars on paper chromatograms. Nature. 1950 Sep 9;166(4219):444–445. doi: 10.1038/166444b0. [DOI] [PubMed] [Google Scholar]
  21. Tanaka S., Fraenkel D. G., Lin E. C. The enzymatic lesion of strain MM-6, a pleiotropic carbohydrate-negative mutant of Escherichia coli. Biochem Biophys Res Commun. 1967 Apr 7;27(1):63–67. doi: 10.1016/s0006-291x(67)80040-8. [DOI] [PubMed] [Google Scholar]
  22. White R. J., Pasternak C. A. The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli. Biochem J. 1967 Oct;105(1):121–125. doi: 10.1042/bj1050121. [DOI] [PMC free article] [PubMed] [Google Scholar]

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