Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1981 Aug;147(2):463–470. doi: 10.1128/jb.147.2.463-470.1981

Substrate specificity of citrate lyase deacetylase of Rhodopseudomonas gelatinosa and Rhodopseudomonas palustris.

F Giffhorn, T Zimmermann, A Kuhn
PMCID: PMC216065  PMID: 6167565

Abstract

Citrate lyase (EC 4.1.3.6) isolated from Rhodopseudomonas palustris was investigated with regard to its kinetic properties and its subunit composition. This enzyme was inactivated by citrate lyase deacetylase (EC 3.1.2.-) of Rhodopseudomonas gelatinosa. A corresponding cross-reaction was measured with partially purified deacetylase of R. palustris and citrate lyase of R. gelatinosa. The three different subunit types (alpha, beta, and gamma) of citrate lyase from R. gelatinosa wee purified to homogeneity, and antibodies were prepared against each of the three subunits and against the native enzyme complex. In corresondence with the enzymatic interactions, immunological cross-reactions were found between anti-enzyme and anti-large subunit antibodies and citrate lyase from R. palustris. On the other hand, no immunological cross-reactions were detectable among each of the antibodies and citrate lyases from Enterobacter aerogenes, Streptococcus diacetilactis, and Clostridium sphenoides. Antibodies against the large subunit of citrate lyase inhibited the deacetylase, but antibodies against the middle and small subunits did not, indicating that the large subunits of citrate lyase are involved in binding the deacetylase.

Full text

PDF
463

Images in this article

465Image
on p.465
466Image
on p.466
466Image
on p.466
466Image
on p.466

Selected References

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

  1. Arnheim N., Prager E. M., Wilson A. C. Immunological prediction of sequence differences among proteins. Chemical comparison of chicken, quail, and phesant lysozymes. J Biol Chem. 1969 Apr 25;244(8):2085–2094. [PubMed] [Google Scholar]
  2. Arnon R. Antibodies to enzymes--a tool in the study of antigenic specificity determinants. Curr Top Microbiol Immunol. 1971;54:47–93. doi: 10.1007/978-3-642-65123-6_3. [DOI] [PubMed] [Google Scholar]
  3. BUCK A. A., MAYER H. COMPARATIVE STUDIES OF THE RAPID PLASMA REAGIN CARD TEST FOR SYPHILIS AND THE VDRL SLIDE TEST IN ETHIOPIA. Am J Hyg. 1964 Jul;80:85–90. doi: 10.1093/oxfordjournals.aje.a120462. [DOI] [PubMed] [Google Scholar]
  4. Bayer E., Eggerer H. On the significance of the prosthetic group composition of citrate lyase. Eur J Biochem. 1978 May;86(1):203–208. doi: 10.1111/j.1432-1033.1978.tb12300.x. [DOI] [PubMed] [Google Scholar]
  5. Beuscher N., Mayer F., Gottschalk G. Citrate lyase from Rhodopseudomonas gelatinosa: purification, electron microscopy and subunit structure. Arch Microbiol. 1974;100(4):307–328. doi: 10.1007/BF00446325. [DOI] [PubMed] [Google Scholar]
  6. Bowen T. J., Mortimer M. G. Sub-units of citrate oxaloacetate-lyase. Eur J Biochem. 1971 Nov 11;23(2):262–266. doi: 10.1111/j.1432-1033.1971.tb01617.x. [DOI] [PubMed] [Google Scholar]
  7. Bowien B., Mayer F. Further studies on the quaternary structure of D-ribulose-1, 5-bisphosphate carboxylase from Alcaligenes eutrophus. Eur J Biochem. 1978 Jul 17;88(1):97–107. doi: 10.1111/j.1432-1033.1978.tb12426.x. [DOI] [PubMed] [Google Scholar]
  8. Buckel W., Buschmeier V., Eggerer H. Der Wirkungsmechanismus der Citrat-Lyase aus Klebsiella aerogenes. Hoppe Seylers Z Physiol Chem. 1971 Sep;352(9):1195–1205. [PubMed] [Google Scholar]
  9. Carpenter D. E., Singh M., Richards E. G., Srere P. A. On the molecular weights of the three nonidentical subunits of citrate lyase from Klebsiella aerogenes. J Biol Chem. 1975 May 10;250(9):3254–3260. [PubMed] [Google Scholar]
  10. Dimroth P., Eggerer H. Isolation of subunits of citrate lyase and characterization of their function in the enzyme complex. Proc Natl Acad Sci U S A. 1975 Sep;72(9):3458–3462. doi: 10.1073/pnas.72.9.3458. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Dimroth P. The prosthetic group of citrate-lyase acyl-carrier protein. Eur J Biochem. 1976 Apr 15;64(1):269–281. doi: 10.1111/j.1432-1033.1976.tb10297.x. [DOI] [PubMed] [Google Scholar]
  12. Giffhorn F., Gottschalk G. Crystallization and subunit composition of citrate lyase of Rhodopseudomonas gelatinosa. FEBS Lett. 1978 Dec 1;96(1):175–178. doi: 10.1016/0014-5793(78)81088-6. [DOI] [PubMed] [Google Scholar]
  13. Giffhorn F., Gottschalk G. Inactivation of citrate lyase from Rhodopseudomonas gelatinosa by a specific deacetylase and inhibition of this inactivation by L-(+1-glutamate. J Bacteriol. 1975 Dec;124(3):1052–1061. doi: 10.1128/jb.124.3.1052-1061.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Giffhorn F., Rode H., Kuhn A., Gottschalk G. Citrate lyase deacetylase of Rhodopseudomonas gelatinosa. Isolation of the enzyme and studies on the inhibition by L-glutamate. Eur J Biochem. 1980 Oct;111(2):461–471. doi: 10.1111/j.1432-1033.1980.tb04961.x. [DOI] [PubMed] [Google Scholar]
  15. Hiremath S. T., Paranjpe S., SivaRaman C. Purification and properties of citrate lyase from Streptococcus faecalis. Biochem Biophys Res Commun. 1976 Oct 4;72(3):1122–1128. doi: 10.1016/s0006-291x(76)80248-3. [DOI] [PubMed] [Google Scholar]
  16. Kümmel A., Behrens G., Gottschalk G. Citrate lyase from Streptococcus diacetilactis. Association with its acetylating enzyme. Arch Microbiol. 1975;102(2):111–116. doi: 10.1007/BF00428354. [DOI] [PubMed] [Google Scholar]
  17. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  18. Lazarides E., Burridge K. Alpha-actinin: immunofluorescent localization of a muscle structural protein in nonmuscle cells. Cell. 1975 Nov;6(3):289–298. doi: 10.1016/0092-8674(75)90180-4. [DOI] [PubMed] [Google Scholar]
  19. Mahadik S. P., SivaRaman C. Citrate lyase: molecular weight and subunit structure. Biochem Biophys Res Commun. 1968 Jul 26;32(2):167–172. doi: 10.1016/0006-291x(68)90364-1. [DOI] [PubMed] [Google Scholar]
  20. Oppenheimer N. J., Singh M., Sweeley C. C., Sung S. J., Srere P. A. The configuration and location of the ribosidic linkage in the prosthetic group of citrate lyase (Klebsiella aerogenes). J Biol Chem. 1979 Feb 25;254(4):1000–1002. [PubMed] [Google Scholar]
  21. Pfennig N. Phototrophic green and purple bacteria: a comparative, systematic survey. Annu Rev Microbiol. 1977;31:275–290. doi: 10.1146/annurev.mi.31.100177.001423. [DOI] [PubMed] [Google Scholar]
  22. Robinson J. B., Jr, Singh M., Srere P. A. Structure of the prosthetic group of Klebsiella aerogenes citrate (pro-3S)-lyase. Proc Natl Acad Sci U S A. 1976 Jun;73(6):1872–1876. doi: 10.1073/pnas.73.6.1872. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Singh M., Carpenter D. E., Srere P. A. Nonidentical subunits of citrate lyase from Klebsiella aerogenes. Biochem Biophys Res Commun. 1974 Aug 19;59(4):1211–1218. doi: 10.1016/0006-291x(74)90443-4. [DOI] [PubMed] [Google Scholar]
  24. Singh M., Robinson J. B., Jr, Srere P. A. On the structure of the prosthetic group of citrate (pro-3S)-lyase. J Biol Chem. 1977 Sep 10;252(17):6061–6068. [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES