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. 1975 Apr;72(4):1268–1271. doi: 10.1073/pnas.72.4.1268

Evolution of biosynthetic pathways: immunological approach.

P Truffa-Bachi, N Guiso, G N Cohen, J Theze, B Burr
PMCID: PMC432513  PMID: 48255

Abstract

Through the use of specific immunoadsorbent columns, it is shown that Escherichia coli aspartokinase I-homoserine dehydrogenase I, aspartokinase II-homoserine dehydrogenase II, aspartokinase III, and homoserine kinase, enzymes involved in the same complex biosynthetic pathway, share antigenic determinants. This raises the question of a common origin for the four cibtenoirart kinases. (Aspartate kinase or ATP:L aspartate 4-phosphotransferase, EC 2.7.2.4; homoserine dehydrogenase or Lhomoserine:NADP oxidoreductase, EC 1.1.1.3; homoserine kinase or ATP:L-homoserine O-phosphotransferase, EC 2.7.1.39.)

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Selected References

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

  1. Costrejean J. M., Guiso N., Cowie D. B., Cohen G. N., Truffa-Bachi P. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Distribution and accessibility to antibodies of some epitopes of the bifunctional enzyme. Eur J Biochem. 1975 Jan 2;50(2):431–435. doi: 10.1111/j.1432-1033.1975.tb09820.x. [DOI] [PubMed] [Google Scholar]
  2. Cowie D. B., Truffa-Bachi P., Costrejean J. M., Py M. C., Cohen G. N. A preliminary immunochemical study of E. coli aspartokinase I-homoserine dehydrogenase I. Biochem Biophys Res Commun. 1973 Jul 2;53(1):188–193. doi: 10.1016/0006-291x(73)91418-6. [DOI] [PubMed] [Google Scholar]
  3. Falcoz-Kelly F., Janin J., Saari J. C., Véron M., Truffa-Bachi P., Cohen G. N. Revised structure of aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12. Evidence for four identical subunits. Eur J Biochem. 1972 Aug 4;28(4):507–519. doi: 10.1111/j.1432-1033.1972.tb01938.x. [DOI] [PubMed] [Google Scholar]
  4. Falcoz-Kelly F., van Rapenbusch R., Cohen G. N. The methionine-repressible homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Preparation of the homogeneous protein catalyzing the two activities. Molecular weight of the native enzyme and of its subunits. Eur J Biochem. 1969 Mar;8(1):146–152. doi: 10.1111/j.1432-1033.1969.tb00507.x. [DOI] [PubMed] [Google Scholar]
  5. Guiso N., Truffa-Bachi P. Enzyme and enzyme fragments purification by specific immunoadsorbents. Application to structural studies of aspartokinase I-homoserine dehydrogenase I of Escherichia coli. Eur J Biochem. 1974 Mar 1;42(2):401–404. doi: 10.1111/j.1432-1033.1974.tb03352.x. [DOI] [PubMed] [Google Scholar]
  6. Horowitz N. H. On the Evolution of Biochemical Syntheses. Proc Natl Acad Sci U S A. 1945 Jun;31(6):153–157. doi: 10.1073/pnas.31.6.153. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Janin J., Cohen G. N. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. A study of the allosteric equilibrium. Eur J Biochem. 1969 Dec;11(3):520–529. doi: 10.1111/j.1432-1033.1969.tb00804.x. [DOI] [PubMed] [Google Scholar]
  8. Janin J., Truffa-Bachi P., Cohen G. N. Subunits of the complex protein carrying the threonine-sensitive aspartokinase activity in a mutant of Escherichia coli K 12. Biochem Biophys Res Commun. 1967 Feb 21;26(4):429–434. doi: 10.1016/0006-291x(67)90564-5. [DOI] [PubMed] [Google Scholar]
  9. Kaminski M., Falcoz-Kelly F., Truffa-Bachi P., Patte J. C., Cohen G. N. The antigenic independence of the three aspartokinases of Escherichia coli K 12. Eur J Biochem. 1969 Dec;11(2):278–282. doi: 10.1111/j.1432-1033.1969.tb00770.x. [DOI] [PubMed] [Google Scholar]
  10. LEWIS E. B. Pseudoallelism and gene evolution. Cold Spring Harb Symp Quant Biol. 1951;16:159–174. doi: 10.1101/sqb.1951.016.01.014. [DOI] [PubMed] [Google Scholar]
  11. Lafuma C., Gros C., Patte J. C. Regulation of the lysine biosynthetic pathway of Escherichia coli K12. Isolation, molecular weight and amino acid analysis of the lysine sensitive aspartokinase. Eur J Biochem. 1970 Jul;15(1):111–115. doi: 10.1111/j.1432-1033.1970.tb00983.x. [DOI] [PubMed] [Google Scholar]
  12. Patte J. C., Le Bras G., Cohen G. N. Regulation by methionine of the synthesis of a third aspartokinase and of a second homoserine dehydrogenase in Escherichia coli K 12. Biochim Biophys Acta. 1967 Mar 22;136(2):245–247. doi: 10.1016/0304-4165(67)90069-4. [DOI] [PubMed] [Google Scholar]
  13. Reichlin M., Bucci E., Fronticelli C., Wyman J., Antonini E., Ioppolo C., Rossi-Fanelli A. The properties and interactions of the isolated alpha- and beta-chains of human haemoglobin. IV. Immunological studies involving antibodies against the isolated chains. J Mol Biol. 1966 May;17(1):18–28. doi: 10.1016/s0022-2836(66)80091-8. [DOI] [PubMed] [Google Scholar]
  14. Richaud C., Mazat J. P., Gros C., Patte J. C. Subunit structure of aspartokinase 3 of Escherichia coli K12. Eur J Biochem. 1973 Dec 17;40(2):619–629. doi: 10.1111/j.1432-1033.1973.tb03234.x. [DOI] [PubMed] [Google Scholar]
  15. Szentirmai A., Szentirmai M., Umbarger H. E. Isoleucine and valine metabolism of Escherichia coli. XV. Biochemical properties of mutants resistant to thiaisoleucine. J Bacteriol. 1968 May;95(5):1672–1679. doi: 10.1128/jb.95.5.1672-1679.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Thèze J., Saint-Girons I. Threonine locus of Escherichia coli K-12: genetic structure and evidence for an operon. J Bacteriol. 1974 Jun;118(3):990–998. doi: 10.1128/jb.118.3.990-998.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Théze J., Kleidman L., St Girons I. Homoserine kinase from Escherichia coli K-12: properties, inhibition by L-threonine, and regulation of biosynthesis. J Bacteriol. 1974 May;118(2):577–581. doi: 10.1128/jb.118.2.577-581.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Véron M., Falcoz-Kelly F., Cohen G. N. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain. Eur J Biochem. 1972 Aug 4;28(4):520–527. doi: 10.1111/j.1432-1033.1972.tb01939.x. [DOI] [PubMed] [Google Scholar]
  19. Wampler D. E., Westhead E. W. Two aspartokinases from Escherichia coli. Nature of the inhibition and molecular changes accompanying reversible inactivation. Biochemistry. 1968 May;7(5):1661–1671. doi: 10.1021/bi00845a007. [DOI] [PubMed] [Google Scholar]

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