Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1978 Mar 15;170(3):487–493. doi: 10.1042/bj1700487

The biochemical pathway for the breakdown of N4-ethyl-L-asparagine in the bacterium Pseudomonas stutzeri.

R W Dineen, D O Gray
PMCID: PMC1183923  PMID: 25650

Abstract

N4-Ethyl-L-[u-14C]asparagine and L-[U-14C]aspartate give identical metabolites, mainly intermediates of the tricarboxylic acid cycle and related amino acids, in whole cells of Pseudomonas stutzeri. The labelled asparagine derivative is converted into [14C]-aspartate by cell-free extracts, and this reaction, which has an optimum pH of 8.8 +/- 0.2, is neither inhibited by unlabelled asparagine nor enhanced by unlabelled 2-oxoglutarate. No labelled keto acid corresponding to N4-ethylasparagine was detected in either whole cells or cell-free extracts. Thus N4-ethyl-L-asparagine, like asparagine, must be broken down by hydrolysis, at least in this bacterium.

Full text

PDF
487

Selected References

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

  1. FOWDEN L. A new asparagine derivative, N4-(2-hydroxy-ethyl)-L-asparagine, from bryony (Bryonia dioica). Biochem J. 1961 Oct;81:154–156. doi: 10.1042/bj0810154. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Firmin J. L., Gray D. O. The biochemical pathway for the breakdown of methyl cyanide (acetonitrile) in bacteria. Biochem J. 1976 Aug 15;158(2):223–229. doi: 10.1042/bj1580223. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. GRAY D. O., FOWDEN L. N-Ethyl-L-asparagine: a new amino-acid amide from Ecballium. Nature. 1961 Feb 4;189:401–402. doi: 10.1038/189401a0. [DOI] [PubMed] [Google Scholar]
  4. Howard J. B., Carpenter F. H. L-asparaginase from Erwinia carotovora. Substrate specificity and enzymatic properties. J Biol Chem. 1972 Feb 25;247(4):1020–1030. [PubMed] [Google Scholar]
  5. MEISTER A., FRASER P. E. Enzymatic formation of L-asparagine by transamination. J Biol Chem. 1954 Sep;210(1):37–43. [PubMed] [Google Scholar]
  6. MEISTER A. Preparation of enzymatic reactions of the keto analogues of asparagine and glutamine. J Biol Chem. 1953 Feb;200(2):571–589. [PubMed] [Google Scholar]
  7. MEISTER A., SOBER H. A., TICE S. V., FRASER P. E. Transamination and associated deamidation of asparagine and glutamine. J Biol Chem. 1952 May;197(1):319–330. [PubMed] [Google Scholar]
  8. RAMADANM EL-D, ELASMAR F., GREENBERG D. M. PURIFICATION AND PROPERTIES OF GLUTAMINASE AND ASPARAGINASE FROM A PSEUDOMONAD. I. PURIFICATION AND PHYSICAL CHEMICAL PROPERTIES. Arch Biochem Biophys. 1964 Oct;108:143–149. doi: 10.1016/0003-9861(64)90365-0. [DOI] [PubMed] [Google Scholar]
  9. Rogers L. J., Shah S. P., Goodwin T. W. Intracellular localization of mevalonate-activating enzymes in plant cells. Biochem J. 1966 May;99(2):381–388. doi: 10.1042/bj0990381. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. TREVELYAN W. E., PROCTER D. P., HARRISON J. S. Detection of sugars on paper chromatograms. Nature. 1950 Sep 9;166(4219):444–445. doi: 10.1038/166444b0. [DOI] [PubMed] [Google Scholar]
  11. Wade H. E., Elsworth R., Herbert D., Keppie J., Sargeant K. A new L-asparaginase with antitumour activity? Lancet. 1968 Oct 5;2(7571):776–777. doi: 10.1016/s0140-6736(68)90977-x. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES