Abstract
The enzyme L-threonine dehydrogenase was demonstrated in extracts of Escherichia coli K-12, and was shown to be the first enzyme of the pathway converting threonine to glycine. The enzyme was induced by L-leucine, but not by its substrate, L-threonine. The metabolic significance of leucine as a catabolic signal for amino acid degradation is considered.
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- Blackmore M. A., Turner J. M. Threonine metabolism via two-carbon compounds by Pseudomonas oxalaticus. J Gen Microbiol. 1971 Aug;67(2):243–246. doi: 10.1099/00221287-67-2-243. [DOI] [PubMed] [Google Scholar]
- Deutch C. E., Soffer R. L. Regulation of proline catabolism by leucyl,phenylalanyl-tRNA-protein transferase. Proc Natl Acad Sci U S A. 1975 Jan;72(1):405–408. doi: 10.1073/pnas.72.1.405. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Fraser J., Newman E. B. Derivation of glycine from threonine in Escherichia coli K-12 mutants. J Bacteriol. 1975 Jun;122(3):810–817. doi: 10.1128/jb.122.3.810-817.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Isenberg S., Newman E. B. Studies on L-serine deaminase in Escherichia coli K-12. J Bacteriol. 1974 Apr;118(1):53–58. doi: 10.1128/jb.118.1.53-58.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lessie T. G., Whiteley H. R. Properties of threonine deaminase from a bacterium able to use threonine as sole source of carbon. J Bacteriol. 1969 Nov;100(2):878–889. doi: 10.1128/jb.100.2.878-889.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- 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]
- Miller B. A., Newman E. B. Control of serine transhydroxymethylase synthesis in Escherichia coli K12. Can J Microbiol. 1974 Jan;20(1):41–47. doi: 10.1139/m74-007. [DOI] [PubMed] [Google Scholar]
- Morris J. G. Utilization of L-threnonine by a pseudomonad: a catabolic role for L-threonine aldolase. Biochem J. 1969 Nov;115(3):603–605. doi: 10.1042/bj1150603. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- PARDEE A. B., PRESTIDGE L. S. Induced formation of serine and threonine deaminases by Escherichia coli. J Bacteriol. 1955 Dec;70(6):667–674. doi: 10.1128/jb.70.6.667-674.1955. [DOI] [PMC free article] [PubMed] [Google Scholar]
- PAZ M. A., BLUMENFELD O. O., ROJKIND M., HENSON E., FURFINE C., GALLOP P. M. DETERMINATION OF CARBONYL COMPOUNDS WITH N-METHYL BENZOTHIAZOLONE HYDRAZONE. Arch Biochem Biophys. 1965 Mar;109:548–559. doi: 10.1016/0003-9861(65)90400-5. [DOI] [PubMed] [Google Scholar]
- Soffer R. L. Aminoacyl-tRNA transferases. Adv Enzymol Relat Areas Mol Biol. 1974;40(0):91–139. doi: 10.1002/9780470122853.ch4. [DOI] [PubMed] [Google Scholar]
- Turner J. M. Microbial metabolism of amino ketones. L-1-aminopropan-2-ol dehydrogenase and L-threonine dehydrogenase in Escherichia coli. Biochem J. 1967 Jul;104(1):112–121. doi: 10.1042/bj1040112. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- URATA G., GRANICK S. Biosynthesis of alpha-aminoketones and the metabolism of aminoacetone. J Biol Chem. 1963 Feb;238:811–820. [PubMed] [Google Scholar]