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. 1983 Oct;156(1):273–280. doi: 10.1128/jb.156.1.273-280.1983

Growth, enzyme levels, and some metabolic properties of an Escherichia coli mutant grown on L-threonine as the sole carbon source.

S A Boylan, E E Dekker
PMCID: PMC215080  PMID: 6413491

Abstract

A mutant of Escherichia coli (designated E. coli SBD-76) that utilizes L-threonine as the sole carbon source was isolated. In contrast with levels in extracts of wild-type cells, the levels of threonine dehydrogenase in extracts of this mutant were 100-fold higher than levels of threonine aldolase or degradative threonine dehydratase. Catabolite repression of threonine dehydrogenase was manifested in wild-type, but not SBD-76, cells. For purposes of isolating enzymes, large quantities of SBD-76 cells with the elevated threonine dehydrogenase level could be grown in a fermentor in modified Fraser medium containing 1% glycerol, rather than in the 0.2% L-threonine minimal medium used to isolate the mutant. SBD-76 cells grown on L-threonine excreted glycine and aminoacetone into the medium, and extracts of the mutant strain catalyzed a quantitative conversion of L-threonine to glycine and aminoacetone.

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Selected References

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

  1. Bell S. C., Turner J. M. Bacterial catabolism of threonine. Threonine degradation initiated by L-threonine-NAD+ oxidoreductase. Biochem J. 1976 May 15;156(2):449–458. doi: 10.1042/bj1560449. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Boylan S. A., Dekker E. E. L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12. J Biol Chem. 1981 Feb 25;256(4):1809–1815. [PubMed] [Google Scholar]
  3. Campbell R. L., Dekker E. E. Formation of D-1-amino-2-propanol from L-threonine by enzymes from Escherichia coli K-12. Biochem Biophys Res Commun. 1973 Jul 17;53(2):432–438. doi: 10.1016/0006-291x(73)90680-3. [DOI] [PubMed] [Google Scholar]
  4. Campbell R. L., Swain R. R., Dekker E. E. Purification, separation, and characterization of two molecular forms of D-1-amino-2-propanol:NAD+ oxidoreductase activity from extracts of Escherichia coli K-12. J Biol Chem. 1978 Oct 25;253(20):7282–7288. [PubMed] [Google Scholar]
  5. ELLIOTT W. H. Amino-acetone; its isolation and role in metabolism. Nature. 1959 Apr 11;183(4667):1051–1052. doi: 10.1038/1831051a0. [DOI] [PubMed] [Google Scholar]
  6. FRASER D., JERREL E. A. The amino acid composition of T3 bacteriophage. J Biol Chem. 1953 Nov;205(1):291–295. [PubMed] [Google Scholar]
  7. Faulkner A., Turner J. M. Microbial metabolism of amino alcohols. Aminoacetone metabolism via 1-aminopropan-2-ol in Pseudomonas sp. N.C.I.B. 8858. Biochem J. 1974 Feb;138(2):263–276. doi: 10.1042/bj1380263. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Feldman D. A., Datta P. Catabolite inactivation of biodegradative threonine dehydratase of Escherichia coli. Biochemistry. 1975 Apr 22;14(8):1760–1767. doi: 10.1021/bi00679a031. [DOI] [PubMed] [Google Scholar]
  9. KRASNA A. I., ROSENBLUM C., SPRINSON D. B. The conversion of L-threonine to the Dg-1-amino-2-propanol of vitamin B12. J Biol Chem. 1957 Apr;225(2):745–750. [PubMed] [Google Scholar]
  10. 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]
  11. Lowe D. A., Turner J. M. Origin of the D-1-aminopropan-2-ol fragment of vitamin B12. J Gen Microbiol. 1970 Nov;64(1):119–122. doi: 10.1099/00221287-64-1-119. [DOI] [PubMed] [Google Scholar]
  12. McGilvray D., Morris J. G. Utilization of L-threonine by a species of Arthrobacter. A novel catabolic role for "aminoacetone synthase". Biochem J. 1969 May;112(5):657–671. doi: 10.1042/bj1120657. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Müller G., Gross R., Siebke G. Zur Frage der Bildung des Isopropanolamin-Anteiles im vitamin B 12. Hoppe Seylers Z Physiol Chem. 1971 Dec;352(12):1720–1722. [PubMed] [Google Scholar]
  14. NEUBERGER A., TAIT G. H. The enzymic conversion of threonine to aminoacetone. Biochim Biophys Acta. 1960 Jun 17;41:164–165. doi: 10.1016/0006-3002(60)90388-7. [DOI] [PubMed] [Google Scholar]
  15. Potter R., Kapoor V., Newman E. B. Role of threonine dehydrogenase in Escherichia coli threonine degradation. J Bacteriol. 1977 Nov;132(2):385–391. doi: 10.1128/jb.132.2.385-391.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. UMBARGER H. E., BROWN B. Threonine deamination in Escherichia coli. II. Evidence for two L-threonine deaminases. J Bacteriol. 1957 Jan;73(1):105–112. doi: 10.1128/jb.73.1.105-112.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]

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