Hostname: page-component-586b7cd67f-tf8b9 Total loading time: 0 Render date: 2024-11-23T12:30:27.596Z Has data issue: false hasContentIssue false
  • English
  • Français

Amino acid catabolism in the nematodes Heligmosomoides polygyrus and Panagrellus redivivus. 1. Removal of the amino group

Published online by Cambridge University Press:  06 April 2009

Barbara D. Grantham  and
J. Barrett
Barbara D. Grantham
Affiliation:
Department of Zoology, University College of Wales, Aberystwth, Dyfed SY23 3DA
J. Barrett
Affiliation:
Department of Zoology, University College of Wales, Aberystwth, Dyfed SY23 3DA
Get access Rights & Permissions [Opens in a new window]

Summary

The major transaminase in Heligmosomoides polygyrus, Panagrellus redivivus and rat liver was the 2-oxoglutarate-glutamate system, with relatively few amino acids acting as donors for the pyruvate-alanine and oxaloacetate–aspartate systems. The relative effectiveness of the different amino acid donors in the three transaminase systems was similar in all three tissues. Both H. polygyrus and P. redivivus can oxidatively deaminate a range of L-amino acids, although D-amino acid oxidase activity was low. Serine and threonine dehydratase activity and histidase activity were present in H. polygyrus and P. redivivus and both nematodes were also able to deaminate glutamine, asparagine and arginine. When NAD(H) was the cofactor the glutamate dehydrogenases of H. polygyrus and P. redivivus showed similar regulatory properties to the mammalian enzyme. However, with NADP(H) the results were anomalous. The capacity of both nematodes to transaminate and oxidatively deaminate amino acids was broadly similar and comparable to mammalian tissue. Glutamate dehydrogenase is probably the major route for deamination in these nematodes. A complete sequence of urea cycle enzymes could not be demonstrated in either P. redivivus or H. polygyrus.

Type
Research Article
Information
Parasitology , Volume 93 , Issue 3 , December 1986 , pp. 481 - 493
Copyright
Copyright © Cambridge University Press 1986

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Barrett, J. (1981). Biochemistry of Parasitic Helminths. London: Macmillan.CrossRefGoogle Scholar
Barrett, J. & Butterworth, P. E. (1984). Acetaldehyde formation by mitochondria from the free-living nematode Panagrellus redivivus. The Biochemical Journal 221, 535–40.CrossRefGoogle ScholarPubMed
Bergmeyer, H. U., Gawehn, K. & Grassl, M. (1974). Glutaminase. In Methods of Enzymatic Analysis (ed. H., Bergmeyer), vol. 1, p. 465. Academic Press: New York.Google Scholar
Burren, C. H. (1980). A method for obtaining large numbers of clean infective larvae of Nemato spiroides dubius. Zeitschrift für Parasitenkunde 62, 111–12.CrossRefGoogle Scholar
Burns, R. O. (1971). l-Threonine deaminase-biosynthetic (Salmonella typhimurium). In Methods in Enzymology, vol. 17B, (ed. H., Tabor and Tabor, C. W.) pp. 555–60. New York: Academic Press.Google Scholar
Ceriotti, G. (1974). Ornithine carbamoyltransferase. In Methods of Enzymatic Analysis (ed. Bergmeyer, H. U.), vol. 2, pp. 691–8. New York, Academic Press.CrossRefGoogle Scholar
Dobson, C. (1961). Certain aspects of the host-parasite relationship of Nematospiroides dubius (Baylis). 1. Resistance of male and female mice to experimental infections. Parasitology 51, 173–9.CrossRefGoogle Scholar
Fahien, L. A. & Cohen, P. P. (1964). A kinetic study of carbamoyl phosphate synthetase. Journal of Biological Chemistry 239, 1925–34.CrossRefGoogle Scholar
Horowitz, R. J. (1978). Temporal variability patterns and the distributional patterns of stream fishes. Ecological Monographs 48, 307–21.CrossRefGoogle Scholar
Magasanik, B., Kaminskas, E. & Kimhi, Y. (1971). Histidase (histidine-ammonia-lyase) (Bacilis subtilis). In Methods in Enzymology (ed. H., Tabor and Tabor, C. W.), vol. 17 B, pp. 47–50. New York: Academic Press.Google Scholar
Moroney, M. J. (1962). Facts from Figures. London: Penguin.Google Scholar
Mustafa, T., Komuniecki, R. & Mettrick, D. F. (1978). Cystolic glutamate dehydrogenase in adult Hymenolepis diminuta (Cestoda). Comparative Biochemistry and Physiology 61B, 219–22.Google Scholar
Newsholme, E. A. & Start, C. (1976). Regulation in Metabolism. New York: Wiley.Google ScholarPubMed
Rainbow, V. M. T. (1972). Studies on the helminth parasites of small mammals with particular reference to the ecology and physiology of Nematospiroides dubius. Ph.D. thesis, University of London.Google Scholar
Ratner, S. (1970 a). Argininosuccinate synthetase (steer liver). In Methods in Enzymology (ed. H., Tabor and Tabor, C. W.), vol. 17A, pp. 298–303. New York: Academic Press.Google Scholar
Ratner, S. (1970 b). Arginino-succinase (steer liver). In Methods in Enzymology (ed. H., Tabor and Tabor, C. W.), vol. 17A, pp. 304–9. New York: Academic Press.Google Scholar
Rhodes, M. B. & Ferguson, D. L. (1973). Haemonchus contortus. Enzymes III. Glutamate dehydrogenase. Experimental Parasitology 34, 100–10.Google Scholar
Schwartz, M. K. (1971). Clinical aspects of arginase. In Methods in Enzymology, vol. 17B, (ed. H., Tabor, and Tabor, C. W.), pp. 857–1. New York: Academic Press.Google Scholar
Suda, M. & Nakagawa, M. (1971). l-Serine dehydratase (rat liver). In Methods in Enzymology, vol. 17B, (ed. H., Tabor and Tabor, C. W.), pp. 346–51. New York: Academic Press.Google Scholar
Wright, D. J. (1975). Studies on nitrogen catabolism in Panagrellus redivivus, Goodey, 1945 (Nematoda:Cephalobidae). Comparative Biochemistry and Physiology 52B, 255–69.Google Scholar
Wright, D. J. & Newall, D. R. (1976). Nitrogen excretion, osmotic and ionic regulation in nematodes. In The Organisation of Nematodes, (ed. Croll, H. A.), pp. 163–210. New York: Academic Press.Google Scholar
Wriston, J. C. (1970). Asparaginase. In Methods in Enzymology (ed. H., Tabor and Tabor, C. W.), vol. 17 A, pp. 732–6. New York: Academic Press.Google Scholar