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. 1977 Aug 15;166(2):209–216. doi: 10.1042/bj1660209

Bacterial catabolism of threonine. Threonine degradation initiated by l-threonine acetaldehyde-lyase (aldolase) in species of Pseudomonas

Stephen C Bell 1,*, John M Turner 1
PMCID: PMC1164997  PMID: 911318

Abstract

1. The route of l-threonine degradation was studied in four strains of the genus Pseudomonas able to grow on the amino acid and selected because of their high l-threonine aldolase activity. Growth and manometric results were consistent with the cleavage of l-threonine to acetaldehyde+glycine and their metabolism via acetate and serine respectively. 2. l-Threonine aldolases in these bacteria exhibited pH optima in the range 8.0–8.7 and Km values for the substrate of 5–10mm. Extracts exhibited comparable allo-l-threonine aldolase activities, Km values for this substrate being 14.5–38.5mm depending on the bacterium. Both activities were essentially constitutive. Similar activity ratios in extracts, independent of growth conditions, suggested a single enzyme. The isolate Pseudomonas D2 (N.C.I.B. 11097) represents the best source of the enzyme known. 3. Extracts of all the l-threonine-grown pseudomonads also possessed a CoA-independent aldehyde dehydrogenase, the synthesis of which was induced, and a reversible alcohol dehydrogenase. The high acetaldehyde reductase activity of most extracts possibly resulted in the underestimation of acetaldehyde dehydrogenase. 4. l-Serine dehydratase formation was induced by growth on l-threonine or acetate+glycine. Constitutively synthesized l-serine hydroxymethyltransferase was detected in extracts of Pseudomonas strains D2 and F10. The enzyme could not be detected in strains A1 and N3, probably because of a highly active `formaldehyde-utilizing' system. 5. Ion-exchange and molecular exclusion chromatography supported other evidence that l-threonine aldolase and allo-l-threonine aldolase activities were catalysed by the same enzyme but that l-serine hydroxymethyltransferase was distinct and different. These results contrast with the specificities of some analogous enzymes of mammalian origin.

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Selected References

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  1. Akhtar M., el-Obeid H. A. Inactivation of serine transhydroxymethylase and threonine aldolase activities. Biochim Biophys Acta. 1972 Mar 8;258(3):791–799. doi: 10.1016/0005-2744(72)90180-5. [DOI] [PubMed] [Google Scholar]
  2. Andrews P. The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochem J. 1965 Sep;96(3):595–606. doi: 10.1042/bj0960595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. 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]
  4. Bell S. C., Turner J. M. Bacterial catabolism of threonine. Threonine degradation initiated by l-threonine hydrolyase (deaminating) in a species of Corynebacterium. Biochem J. 1977 Jun 15;164(3):579–587. doi: 10.1042/bj1640579. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dainty R. H., Peel J. L. Biosynthesis of amino acids in Clostridium pasteurianum. Biochem J. 1970 Apr;117(3):573–584. doi: 10.1042/bj1170573. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Dainty R. H. Purification and properties of threonine aldolase from Clostridium pasteurianum. Biochem J. 1970 Apr;117(3):585–592. doi: 10.1042/bj1170585. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Halvorson H. Utilization of single L-amino acids as sole source of carbon and nitrogen by bacteria. Can J Microbiol. 1972 Nov;18(11):1647–1650. doi: 10.1139/m72-255. [DOI] [PubMed] [Google Scholar]
  8. Higgins I. J., Pickard M. A., Turner J. M. Aminoacetone formation and utilization by pseudomonads grown on DL-1-aminopropan-2-ol. J Gen Microbiol. 1968 Nov;54(1):105–114. doi: 10.1099/00221287-54-1-105. [DOI] [PubMed] [Google Scholar]
  9. Jones A., Turner J. M. Microbial metabolism of amino alcohols. 1-Aminopropan-2-ol and ethanolamine metabolism via propionaldehyde and acetaldehyde in a species of Pseudomonas. Biochem J. 1973 May;134(1):167–182. doi: 10.1042/bj1340167. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Jordan P. M., Akhtar M. The mechanism of action of serine transhydroxymethylase. Biochem J. 1970 Jan;116(2):277–286. doi: 10.1042/bj1160277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. KORNBERG H. L., GOTTO A. M. The metabolism of C2 compounds in micro-organisms. 6. Synthesis of cell constituents from glycollate by Pseudomonas sp. Biochem J. 1961 Jan;78:69–82. doi: 10.1042/bj0780069. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. KORNBERG H. L., MORRIS J. G. THE UTILIZATION OF GLYCOLLATE BY MICROCOCCUS DENITRIFICANS: THE BETA-HYDROXYASPARTATE PATHWAY. Biochem J. 1965 Jun;95:577–586. doi: 10.1042/bj0950577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kumagai H., Nagate T., Yoshida H., Yamada H. Threonine aldolase from Candida humicola. II. Purification, crystallization and properties. Biochim Biophys Acta. 1972 Mar 8;258(3):779–790. doi: 10.1016/0005-2744(72)90179-9. [DOI] [PubMed] [Google Scholar]
  14. Kumagai T., Omuda T., Nakaoka A., Yoshimura T. [A study on the quantity of amniotic fluid in the air passages and in the stomach]. Kango. 1972 Mar;24(3):164–166. [PubMed] [Google Scholar]
  15. MORRIS J. G. THE ASSIMILATION OF 2-C COMPOUNDS OTHER THAN ACETATE. J Gen Microbiol. 1963 Aug;32:167–170. doi: 10.1099/00221287-32-2-167. [DOI] [PubMed] [Google Scholar]
  16. 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]
  17. 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]
  18. Newman E. B., Kapoor V., Potter R. Role of L-threonine dehydrogenase in the catabolism of threonine and synthesis of glycine by Escherichia coli. J Bacteriol. 1976 Jun;126(3):1245–1249. doi: 10.1128/jb.126.3.1245-1249.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Ning C., Gest H. Regulation of L-isoleucine biosynthesis in the photosynthetic bacterium rhodospirillum rubrum. Proc Natl Acad Sci U S A. 1966 Dec;56(6):1823–1827. doi: 10.1073/pnas.56.6.1823. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. 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]
  21. Palekar A. G., Tate S. S., Meister A. Rat liver aminomalonate decarboxylase. Identity with cytoplasmic serine hydroxymethylase and allothreonine aldolase. J Biol Chem. 1973 Feb 25;248(4):1158–1167. [PubMed] [Google Scholar]
  22. Pickard M. A., Higgins I. J., Turner J. M. Purification and properties of l-1-aminopropan-2-ol. NAD oxidoreductase from a pseudomonad grown on DL-1-aminopropan-2-ol. J Gen Microbiol. 1968 Nov;54(1):115–126. doi: 10.1099/00221287-54-1-115. [DOI] [PubMed] [Google Scholar]
  23. RajBhandary U. L., Stuart A., Hoskinson R. M., Khorana H. G. Studies on polynucleotides. 78. Yeast phenylalanine transfer ribonucleic acid: terminal sequences. J Biol Chem. 1968 Feb 10;243(3):565–574. [PubMed] [Google Scholar]
  24. Riario-Sforza G., Pagani R., Marinello E. Threonine aldolase and allothreonine aldolase in rat liver. Eur J Biochem. 1969 Mar;8(1):88–92. doi: 10.1111/j.1432-1033.1969.tb00499.x. [DOI] [PubMed] [Google Scholar]
  25. Yamada H., Kumagai H., Nagate T., Yoshida H. Crystalline threonine aldolase from Candida humicola. Biochem Biophys Res Commun. 1970 Apr 8;39(1):53–58. doi: 10.1016/0006-291x(70)90756-4. [DOI] [PubMed] [Google Scholar]

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