1887

Abstract

Various micro-organisms were studied for their thymidine kinase (adenosine 5'-triphosphate: thymidine 5′-phosphotransferase, EC 2.7.1.21) (TK) activity. The sonicated cell extract of Escherichia coli K12 had a TK activity of 35-66 pmol thymidine monophosphate formed min (mg protein). The cell extracts of Salmonella typhimurium and Klebsiella pneumoniae showed a markedly higher (5- to 11-fold) TK activity. Somewhat lower but significant TK activity was detected in the cell extracts of Staphylococcus aureus, Streptococcus pyogenes, Bacillus subtilis and Proteus mzrabilis. In contrast, weak TK activity, if any, was detected in the cell extracts of Pseudomonas aeruginosa. This was also the case with respect to the cell extracts of various actinomycetes (such as Nocardia and Streptomyces) and related organisms (such as Corynebacterium, Mycobacteriurn and Rhodococcus).

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-130-7-1863
1984-07-01
2024-04-26
Loading full text...

Full text loading...

/deliver/fulltext/micro/130/7/mic-130-7-1863.html?itemId=/content/journal/micro/10.1099/00221287-130-7-1863&mimeType=html&fmt=ahah

References

  1. Ellims P. H., Van Der Weyden M. B. 1980; Human liver thymidine kinase.Purification and some properties of the enzyme. Journal of Biological Chemistry 255:11290–11295
    [Google Scholar]
  2. Ellims P. H., Van Der Weyden M. B. 1981; Kinetic mechanism and inhibition of human liver thymidine kinase. Biochimica et biophysica acta 660:238–242
    [Google Scholar]
  3. Goodfellow M. 1971; Numerical taxonomy of some nocardioform bacteria. Journal of General Microbiology 69:33–80
    [Google Scholar]
  4. Grivell A. R., Jackson J. F. 1968; Thymidine kinase: evidence for its absence from Neurosporacrassa and some other micro-organisms, and the relevance of this to the specific labelling of deoxyribonucleic acid. Journal of General Microbiology 54:307–317
    [Google Scholar]
  5. Guirard B. M., Snell E. E. 1981; Biochemical factors in growth. In Manual of Methods For General Bacteriology pp. 79–111 Gerhardt P., Murray R. G. E., Costilow R. N., Nester E. W., Wood W. A., Krieg N. R., Phillips G. B. Edited by Washington :: American Society for Microbiology.;
    [Google Scholar]
  6. Hatch T. P. 1976; Utilization of exogenous thymidine by Chlamydia psittaci growing in thymidine kinase-containing and thymidine kinase-deficient L cells. Journal of Bacteriology 125:706–712
    [Google Scholar]
  7. Hotta Y., Stern H. 1963; Molecular factors of mitotic regulation, I. Synthesis of thymidine kinase. Proceedings of the National Academy of Sciences of the United States of America 49:648–654
    [Google Scholar]
  8. Hopgood M. F., Ballard F. J. 1974; The relative stability of liver cytosol enzymes incubated in vitro. Biochemical Journal 144:371–376
    [Google Scholar]
  9. Kizer D. E., Holman L. 1974; Purification and properties of thymidine kinase from generating rat liver. Biochimica et biophysica acta 350:193–200
    [Google Scholar]
  10. Liu C., Hermann T., Miller P. A. 1977; Feedback inhibition of the synthesis of an antibiotic: Aurodox (X-5108). Journal of Antibiotics 30:244–251
    [Google Scholar]
  11. Madhav R., Coetzee M. L., Ove P. 1980; Purification of thymidine kinase by affinity chromatography with an enzyme inhibitor as the ligand. Archives of Biochemistry and Biophysics 200:99–107
    [Google Scholar]
  12. Mathews C. K., Cohen S. S. 1963; Inhibition of phage-induced thymidylatesynthetase by 5-fluoro- deoxyuridylate. Journal of Biological Chemistry 238:367–370
    [Google Scholar]
  13. Michrina C. A., Deering R. A. 1980; Thymidine kinase activity in Dictyostelium discoideum. Journal of General Microbiology 119:263–266
    [Google Scholar]
  14. Mizuno S. 1969; Fractionation of nucleic acids. In Methodology for Biochemistry: [A-2] Separation, Purification, and Measurement of Nucleic Acids pp. 16–67 Uritani I., Shimura H., Nakamura M., Funazu M. Edited by Tokyo:: Tokyo University Press.;
    [Google Scholar]
  15. Okazaki R., Kornberg A. 1964a; Deoxythymidine kinase of Escherichia coli. I. Purification and some properties of the enzyme. Journal of Biological Chemistry 239:269–274
    [Google Scholar]
  16. Okazaki R., Kornberg A. 1964b; Deoxythymidine kinase of Escherichia coli II. Kinetics and feedback control. Journal of Biological Chemistry 239:275–284
    [Google Scholar]
  17. Stock D. A., Gentry G. A. 1971; Thymidine metabolism in Mycoplasma hominis. Journal of General Microbiology 65:105–107
    [Google Scholar]
  18. Takeya K., Shimamoto M., Mizuguchi Y. 1978; Physicochemical and biological properties of myco- bacteriocin M12 produced by Mycobacterium smegmatis ATCC 25855. Journal of General Microbiology 109:215–223
    [Google Scholar]
  19. Wachsman J. T., Morgan D. D. 1971; Deoxyribonucleoside kinases of Bacillus megaterium KM. Journal of Bacteriology 105:787–792
    [Google Scholar]
  20. Wayne L. G., Doubek J. R., Russell R. L. 1964; Classification and identification of mycobacteria I. Tests employing Tween 80 as substrate. American Review of Respiratory Disease 90:588–597
    [Google Scholar]
  21. Yagil E., Rosner A. 1970; Effect of adenosine and deoxyadenosine on the incorporation and breakdown of thymidine in Escherichia coli K-12. Journal of Bacteriology 103:417–421
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-130-7-1863
Loading
/content/journal/micro/10.1099/00221287-130-7-1863
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