1887

Abstract

SUMMARY: AMP is catabolized by cell-free extracts of to inosine via adenosine by AMP nucleotidase and adenosine deaminase. In the presence of ATP, the AMP nucleotidase is inhibited and an AMP deaminase is activated, resulting in formation of IMP. When low concentrations of ATP are used, the IMP is converted, simultaneously with ATP consumption, to inosine by IMP nucleotidase, which is presumably ATP-sensitive. Since 5′-nucleotidases from various organisms are known to catabolize several ribonucleoside monophosphates, the AMP and IMP nucleotidase activities of may be due to the same enzyme. CTP, GTP and UTP inhibit AMP nucleotidase from without stimulating AMP deaminase, thus severely decreasing the rate of AMP breakdown.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-100-1-5
1977-05-01
2021-10-16
Loading full text...

Full text loading...

/deliver/fulltext/micro/100/1/mic-100-1-5.html?itemId=/content/journal/micro/10.1099/00221287-100-1-5&mimeType=html&fmt=ahah

References

  1. Atkinson D. E. 1968; The energy charge of the adenylate pool as a regulatory parameter. Interaction with feedback modifiers. Biochemistry 7:4030–4034
    [Google Scholar]
  2. Boosman A., Chilson O. P. 1976; Subunit structure of AMP-deaminase from chicken and rabbit skeletal muscle. Journal of Biological Chemistry 251:1847–1852
    [Google Scholar]
  3. Burger R., Lowenstein J. M. 1967; Adenylate deaminase. III. Regulation of deamination pathways in extracts of rat heart and lung. Journal of Biological Chemistry 242:5281–5288
    [Google Scholar]
  4. Chapman A. G., Atkinson D. E. 1973; Stabilization of adenylate energy charge by the adenylate deaminase reaction. Journal of Biological Chemistry 248:8309–8312
    [Google Scholar]
  5. Chapman A. G., Fall L., Atkinson D. E. 1971; Adenylate energy charge in Escherichia coli during growth and starvation. Journal of Bacteriology 108:1072–1086
    [Google Scholar]
  6. Drummond G. I., Yamamoto M. 1971; Nucleotide phosphomonoesterases. In The Enzymes 4, 3rd edn. pp. 337–354 Boyer P. D. Edited by London and New York: Academic Press;
    [Google Scholar]
  7. Felicioli R. A., Senesi S., Marmocchi F., Falcone G., Ipata P. L. 1973; Nucleoside phosphomonoesterases during growth cycle of Bacillus suhtilis. Biochemistry 12:547–552
    [Google Scholar]
  8. Gornall A. G., Bardawill C. J., David M. M. 1949; Determination of serum proteins by means of the biuret reaction. Journal of Biological Chemistry 177:751–766
    [Google Scholar]
  9. Heppel L. A. 1971; The concept of periplasmic enzymes. In Structure and Functionof Biological Membranes pp. 223–247 Rothman L. I. Edited by London and New York: Academic Press;
    [Google Scholar]
  10. Hurwitz J., Heppel L. A., Horecker B. L. 1957; The enzymatic cleavage of adenylic acid to adenine and ribose 5-phosphate. Journal of Biological Chemistry 226:525–540
    [Google Scholar]
  11. Ipata P. L., Palmarini C. A., Senesi S., Falcone G., Felicioli R. 1975; The role of nucleoside triphosphates in the control of 3′- and 5′-AMP dephosphorylation in crude extracts of B. subtilis. FEBS Letters 57:195–197
    [Google Scholar]
  12. Knowles C. J. 1977; Microbial metabolic regulation by adenine nucleotide pools. Symposia of the Society for General Microbiology 27:241–283
    [Google Scholar]
  13. Koch A. L., Vallee G. 1959; The properties of adenosine deaminase and adenosine nucleoside phosphorylase in extracts of Escherichia coli. Journal of Biological Chemistry 234:1213–1218
    [Google Scholar]
  14. Kohn J., Reis J. L. 1963; Bacterial nucleotidases. Journal of Bacteriology 86:713–716
    [Google Scholar]
  15. Makarewicz W., Stankiewicz A. 1976; Purification of AMP-deaminase from human skeletal muscle on 5′-AMP Sepharose 4B. International Journal of Biochemistry 7:245–247
    [Google Scholar]
  16. Niven D. F., Collins P. A., Knowles C. J. 1977; Adenylate energy charge during batch culture of Beneckea natriegens. Journal of General Microbiology 98:95–108
    [Google Scholar]
  17. Schramm V. L., Lazorik F. C. 1975; The pathway of adenylate catabolism in Azotobacter vinelandii. Evidence for adenosine monophosphate nucleosidase as the regulatory enzyme. Journal of Biological Chemistry 250:1801–1808
    [Google Scholar]
  18. Schramm V. L., Leung H. 1973; Regulation of adenosine monophosphate levels as a function of adenosine triphosphate and inorganic phosphate. A proposed metabolic role for adenosine monophosphate nucleosidase from Azotobacter vinelandii. Journal of Biological Chemistry 248:8313–8315
    [Google Scholar]
  19. Smith H. O., Kelly T. J., Roy P. H. 1974; Enzymatic methods for sequence analysis applied to DNA restriction and methylation sites. Methods in Enzymology 29:282–294
    [Google Scholar]
  20. Smith L. D., Kizer D. E. 1969; Purification and properties of rat liver AMP deaminase. Biochimica et biophysica acta 191:415–424
    [Google Scholar]
  21. Weston J. A., Knowles C. J. 1973; A soluble CO-binding c-type cytochrome from the marine bacterium Beneckea natriegens. Biochimica et biophysica acta 305:11–18
    [Google Scholar]
  22. Weston J. A., Knowles C. J. 1974; The respiratory system of the marine bacterium Beneckea natriegens. I. Cytochrome composition. Biochimica et biophysica acta 333:228–236
    [Google Scholar]
  23. Woods H. F., Eggleston L. V., Krebs H. A. 1970; The cause of hepatic accumulation of fructose-I-phosphate on fructose loading. Biochemical Journal 119:501–510
    [Google Scholar]
  24. Yagil E., Beacham I. R. 1975; Uptake of adenosine 5′-monophosphate by Escherichia coli. Journal of Bacteriology 121:401–405
    [Google Scholar]
  25. Yates M. G. 1969; A non-specific adenine nucleotide deaminase from Desulfovibrio desulfuricans. Biochimica et biophysica acta 171:299–310
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-100-1-5
Loading
/content/journal/micro/10.1099/00221287-100-1-5
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

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