Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1966 May;99(2):427–433. doi: 10.1042/bj0990427

Microbial metabolism of amino ketones. Aminoacetone formation from 1-aminopropan-2-ol by a dehydrogenase in Escherichia coli

J M Turner 1
PMCID: PMC1265012  PMID: 5329339

Abstract

1. Washed-cell suspensions of Escherichia coli, incubated at the optimum pH of 6·4 and with a saturating substrate concentration of approx. 10mm, convert dl-1-aminopropan-2-ol into aminoacetone at a rate of approx. 4·0mμmoles/mg. dry wt. of cells/min. at 30°. 2. Mg2+, Mn2+, Co2+, Zn2+, Ca2+, K+ and NH4+, as sulphates, and EDTA have no effect on this rate, although Cu2+ inhibits and Fe2+ activates to some extent. 3. Conditions of growth markedly affect the rate of aminoacetone production by cell suspensions. 4. Dialysed cell-free extracts of E. coli exhibit 1-aminopropan-2-ol-dehydrogenase activity, the enzyme having optimum activity at pH7·0, a requirement for NAD+ and K+, and a Km for the amino alcohol substrate of 0·8mm, calculated for a single enantiomorph. 5. Under optimum conditions 1-aminopropan-2-ol dehydrogenase forms aminoacetone at rate of approx. 3·0mμmoles/mg. of protein/min. at 37°. The enzyme is only slightly inhibited by dl-3-hydroxybutyrate and dl-2-hydroxy-2-phenylethyl-amine. 6. l-Threonine-dehydrogenase activity is exhibited by both whole cells and cell-free extracts. Whole cells produce aminoacetone from l-threonine more slowly than they do from dl-1-aminopropan-2-ol, whereas the situation is reversed in cell-free extracts. Both kinetic evidence, and the fact that synthesis of 1-aminopropan-2-ol dehydrogenase, but not of threonine dehydrogenase, is repressed by compounds such as glucose and pyruvate, provide evidence that the amino alcohol is oxidized by a specific enyme. 7. The metabolic role of 1-aminopropan-2-ol dehydrogenase is discussed.

Full text

PDF
428

Selected References

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

  1. 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]
  2. ELLIOTT W. H. Aminoacetone formation by Staphylococcus aureus. Biochem J. 1960 Mar;74:478–485. doi: 10.1042/bj0740478. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. ELLIOTT W. H. The estimation of aminoacetone and 5-aminolaevulic acid. Biochem J. 1960 Jan;74:90–94. doi: 10.1042/bj0740090. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. GOTTLIEB S. F., MANDEL M. Utilization of 1-amino-2-propanol by a soil bacterium. Can J Microbiol. 1959 Aug;5:363–368. doi: 10.1139/m59-045. [DOI] [PubMed] [Google Scholar]
  5. Green M. L., Elliott W. H. The enzymic formation of aminoacetone from threonine and its further metabolism. Biochem J. 1964 Sep;92(3):537–549. doi: 10.1042/bj0920537. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Green M. L. The activation of L-threonine dehydrogenase by potassium ions. Biochem J. 1964 Sep;92(3):550–555. doi: 10.1042/bj0920550. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. HARTSHORNE D., GREENBERG D. M. STUDIES ON LIVER THREONINE DEHYDROGENASE. Arch Biochem Biophys. 1964 Apr;105:173–178. doi: 10.1016/0003-9861(64)90250-4. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. MAUZERALL D., GRANICK S. The occurrence and determination of delta-amino-levulinic acid and porphobilinogen in urine. J Biol Chem. 1956 Mar;219(1):435–446. [PubMed] [Google Scholar]
  10. NEUBERGER A. Aspects of the metabolism of glycine and of porphyrins. Biochem J. 1961 Jan;78:1–10. doi: 10.1042/bj0780001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. NEUBERGER A., TAIT G. H. Production of aminoacetone by Rhodopseudomonas spheroides. Biochem J. 1962 Aug;84:317–328. doi: 10.1042/bj0840317. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. SHUSTER L. The determination of delta -aminolaevulic acid. Biochem J. 1956 Sep;64(1):101–106. doi: 10.1042/bj0640101. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. URATA G., GRANICK S. Biosynthesis of alpha-aminoketones and the metabolism of aminoacetone. J Biol Chem. 1963 Feb;238:811–820. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES