1887

Abstract

The regulation of the six enzymes responsible for the conversion of aspartate to lysine, together with homoserine dehydrogenase, was studied in In addition to aspartate kinase activity, the synthesis of diaminopimelate decarboxylase was also found to be regulated. The specific activity of this enzyme was reduced to one-third in extracts of cells grown in the presence of lysine. Aspartate-semialdehyde dehydrogenase, dihydrodipicolinate synthase, dihydrodipicolinate reductase, and diaminopimelate dehydrogenase were neither influenced in their specific activity, nor inhibited, by any of the aspartate family of amino acids. Homoserine dehydrogenase was repressed by methionine (to 15% of its original activity) and inhibited by threonine (4% remaining activity). Inclusion of leucine in the growth medium resulted in a twofold increase of homoserine dehydrogenase specific activity. The flow of aspartate semialdehyde to either lysine or homoserine was influenced by the activity of homoserine dehydrogenase or dihydrodipicolinate synthase. Thus, the twofold increase in homoserine dehydrogenase activity resulted in a decrease in lysine formation accompanied by the formation of isoleucine. In contrast, repression of homoserine dehydrogenase resulted in increased lysine formation. A similar increase of the flow of aspartate semialdehyde to lysine was found in strains with increased dihydrodipicolinate synthase activity, constructed by introducing the gene of (coding for the synthase) into

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-134-12-3221
1988-12-01
2024-04-25
Loading full text...

Full text loading...

/deliver/fulltext/micro/134/12/mic-134-12-3221.html?itemId=/content/journal/micro/10.1099/00221287-134-12-3221&mimeType=html&fmt=ahah

References

  1. Bartlett A.T.M., White P.J. 1986; Regulation of the enzymes of lysine biosynthesis in Bacillus sphaericus NCTC9602 during vegetative growth.. Journal of General Microbiology 132:3169–3177
    [Google Scholar]
  2. Birnboim H.C., Doly J. 1979; A rapid alkaline extraction procedure for screening recombinant plasmid DNA.. Nucleic Acids Research 7:1513–1523
    [Google Scholar]
  3. Black S., Wright N.G. 1955; Aspartic β- semialdehyde dehydrogenase and aspartic ^-semi- aldehyde.. Journal of Biological Chemistry 213:39–50
    [Google Scholar]
  4. Bukhari A.I., Taylor A.L. 1971; Genetic analysis of diaminopimelic acid and lysine-requiring mutants of Escherichia coli. . Journal of Bacteriology 105:844–854
    [Google Scholar]
  5. Follettie M.T., Yeh P., Shink H.K., Peoples O.P., Han K.S., Sinskey A.J. 1986; Development of recombinant DNA technology for Corynebacterium glutamicum: isolation and characterization of amino acid biosynthetic genes.. Fifth International Symposium on the Genetics of Industrial Microorganisms, Split, Jugoslavia p. 128 abstract
    [Google Scholar]
  6. Hanahan D. 1985; Techniques for transformation of Escherichia coli. . In DNA Cloning 1 pp 109–136 Glover D. M. Edited by Oxford & Washington: IRL Press;
    [Google Scholar]
  7. Hegemann G.D., Cohen G.N., Morgan R. 1970; Aspartic semialdehyde dehydrogenase.. Methods in Enzymology 17A:708–713
    [Google Scholar]
  8. Kinoshita S. 1985; Glutamic acid bacteria.. In Biology of Industrial Microorganisms pp 116–142 Weinheim: Verlag Chemie;
    [Google Scholar]
  9. Kleemann A., Leuchtenberger W., Hoppe B., Tanner H. 1985; Amino acids.. In Ullmann’s Encyclopedia of Industrial Chemistry A2 pp 57–97 Weinheim: VCH-Verlagsgesellschaft;
    [Google Scholar]
  10. Maniatis T., Fritsch E.F., Sambrook J. 1982 Molecular Cloning: a Laboratory Manual Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  11. Misono H., Togawa H., Yamamoto T., Soda K. 1979; meso-2,6-Diaminopimelate d-dehydrogen- ase: distribution and the reaction product.. Journal of Bacteriology 137:22–27
    [Google Scholar]
  12. Miyajima R., Shiio I. 1971; Regulation of aspartate family amino acid biosynthesis in Brevi- bacterium flavum. IV. Repression of the enzymes in threonine biosynthesis.. Agricultural and Biological Chemistry 35:424–430
    [Google Scholar]
  13. Miyajima R., Otsuka S.I., Shiio I. 1968; Regulation of aspartate family amino acid biosynthesis in Brevibacterium flavum. I. Inhibition by amino acids of the enzymes in threonine biosynthesis.. Journal of Biochemistry 63:139–148
    [Google Scholar]
  14. Nakayama K., Tanaka H., Hagino H., Kinoshita S. 1966; Studies on lysine fermentation. V. Concerted feedback inhibition of aspartokinase and the absence of lysine inhibition on aspartic semialdehyde-pyruvate condensation in Micrococcus glutamicus. . Agricultural and Biological Chemistry 30:611–616
    [Google Scholar]
  15. Patte J.-C. 1983; Diaminopimelate and lysine.. In Amino Acids, Biosynthesis and Genetic Regulation pp 213–228 Hermann K. M., Somerville R. L. Edited by London & Amsterdam: Addison- Wesley;
    [Google Scholar]
  16. Richaud F., Richaud C., Ratet P., Patte J.-C. 1986; Chromosomal location and nucleotide sequence of the Escherichia coli dapA gene.. Journal of Bacteriology 166:297–300
    [Google Scholar]
  17. Sano K., Shiio I. 1970; Microbial production of L- lysine. III. Production by mutants resistant to S-(2- aminoethyl)-l-cysteine.. Journal of General and Applied Microbiology 16:373–391
    [Google Scholar]
  18. Shiio I., Miyajima R. 1969; Concerted inhibition and its reversal by end products of aspartate kinase in Brevibacterium flavum. . Journal of Biochemistry 65:849–859
    [Google Scholar]
  19. Shiio I., Sano K. 1969; Microbial production of l- lysine. II. Production by mutants sensitive to threonine or methionine.. Journal of General and Applied Microbiology 15:267–287
    [Google Scholar]
  20. Shiio I., Miyajima R., Sano K. 1970; Genetically desensitized aspartate kinase to the concerted feedback inhibition in Brevibacterium flavum. . Journal of Biochemistry 68:701–710
    [Google Scholar]
  21. Stragier P., Richaud F., Borne F., Patte J.-C. 1983; Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli. I. Identification of a lysR gene encoding an activator of the lysA gene.. Journal of Molecular Biology 168:307–320
    [Google Scholar]
  22. Thierbach G., Schwarzer A., Pühler A. 1988; Transformation of spheroplasts and protoplasts in Corynebacterium glutamicum. . European Journal of Applied Microbiology and Biotechnology in the Press
    [Google Scholar]
  23. Tosaka O., Takinami K. 1978; Pathway and regulation of lysine biosynthesis in Brevibacterium lactofermentum. . Agricultural and Biological Chemistry 42:95–100
    [Google Scholar]
  24. Tosaka O., Takinami K., Hirose Y. 1978a; l- Lysine production by 5-(2-aminoethyl>L-cysteine and α-amino-β-hydroxyvaleric acid resistant mutants of Brevibacterium lactofermentum. . Agricultural and Biological Chemistry 42:745–752
    [Google Scholar]
  25. Tosaka O., Hirakawa H., Takinami K., Hirose Y. 1978b; Regulation of lysine biosynthesis by leucine in Brevibacterium lactofermentum. . Agricultural and Biological Chemistry 42:1501–1506
    [Google Scholar]
  26. Tosaka O., Ishihara M., Morinaga Y., Takinami K. 1979; Mode of conversion of asparto β- semialdehyde to l-threonine and l-lysine in Brevibacterium lactofermentum. . Agricultural and Biological Chemistry 43:265–270
    [Google Scholar]
  27. White P.J. 1983; The essential role of diaminopimelate dehydrogenase in the biosynthesis of lysine by Bacillus sphaericus. . Journal of General Microbiology 129:739–749
    [Google Scholar]
  28. Yeh P., Sicard A.M., Sinskey A.J. 1988a; General organization of the genes specifically involved in the diaminopimelate-lysine biosynthetic pathway of Corynebacterium glutamicum. . Molecular and General Genetics 212:105–111
    [Google Scholar]
  29. Yeh P., Sicard A.M., Sinskey A.J. 1988b; Nucleotide sequence of the lysA gene of Corynebacterium glutamicum and possible mechanisms for modulation of its expression.. Molecular and General Genetics 212:112–119
    [Google Scholar]
  30. Yamaguchi K., Ishino S., Araki K., Shirahata K. 1986; 3C NMR studies of lysine fermentation with a Corynebacterium glutamicum mutant.. Agricultural and Biological Chemistry 50:2453–2459
    [Google Scholar]
  31. Yamakura F., Ikeda Y., Kimura K., Sasakawa T. 1974; Partial purification and some properties of pyruvate-aspartic semialdehyde condensing enzyme from sporulating Bacillus subtilis. . Journal of Biochemistry 76:611–621
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-134-12-3221
Loading
/content/journal/micro/10.1099/00221287-134-12-3221
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error