Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1981 Jul;147(1):101–109. doi: 10.1128/jb.147.1.101-109.1981

Biosynthesis of bacterial glycogen: purification and structural properties of Rhodospirillum tenue adenosine diphosphate glucose synthetase.

S G Yung, J Preiss
PMCID: PMC216013  PMID: 6263861

Abstract

Adenosine diphosphate glucose synthetase from the photosynthetic bacterium Rhodospirillum tenue has been purified greater than 95%. The molecular weight of the enzyme is approximately 215,000, with a subunit molecular weight of about 51,000. The enzyme appears to be composed of four similar if not identical subunits. Although the amino acid composition of the enzyme is similar to that of Escherichia coli and Salmonella typhimurium, no apparent homology has been observed between their N-terminal amino acid sequences. Antisera prepared against the R. tenue enzyme can partially inhibit the activities of adenosine diphosphate glucose synthetases from other photosynthetic bacteria.

Full text

PDF
101

Images in this article

106Image
on p.106

Selected References

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

  1. CRESTFIELD A. M., MOORE S., STEIN W. H. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J Biol Chem. 1963 Feb;238:622–627. [PubMed] [Google Scholar]
  2. Cocks G. T., Wilson A. C. Enzyme evolution in the Enterobacteriaceae. J Bacteriol. 1972 Jun;110(3):793–802. doi: 10.1128/jb.110.3.793-802.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry. 1967 Jul;6(7):1948–1954. doi: 10.1021/bi00859a010. [DOI] [PubMed] [Google Scholar]
  4. Furlong C. E., Preiss J. Biosynthesis of bacterial glycogen. VII. Purification and properties of the adenosine diphosphoglucose pyrophosphorylase of Rhodospirillium rubrum. J Biol Chem. 1969 May 25;244(10):2539–2548. [PubMed] [Google Scholar]
  5. Ghosh H. P., Preiss J. Adenosine diphosphate glucose pyrophosphorylase. A regulatory enzyme in the biosynthesis of starch in spinach leaf chloroplasts. J Biol Chem. 1966 Oct 10;241(19):4491–4504. [PubMed] [Google Scholar]
  6. Haugen T. H., Ishaque A., Preiss J. Biosynthesis of bacterial glycogen. Characterization of the subunit structure of Escherichia coli B glucose-1-phosphate adenylyltransferase (EC 2.7.7.27). J Biol Chem. 1976 Dec 25;251(24):7880–7885. [PubMed] [Google Scholar]
  7. Haugen T., Ishaque A., Chatterjee A. K., Preiss J. Purification of Escherichia coli ADPglucose pyrophosphorylase by affinity chromatography. FEBS Lett. 1974 Jun 1;42(2):205–208. doi: 10.1016/0014-5793(74)80786-6. [DOI] [PubMed] [Google Scholar]
  8. Kulbe K. D. Micropolyamide thin-layer chromatography of phenylthiohydantoin amino acids (PTH) at subnanomolar level. A rapid microtechnique for simultaneous multisample identification after automated Edman degradations. Anal Biochem. 1974 Jun;59(2):564–573. doi: 10.1016/0003-2697(74)90310-8. [DOI] [PubMed] [Google Scholar]
  9. 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]
  10. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  11. Lehmann M., Preiss J. Biosynthesis of bacterial glycogen: purification and properties of Salmonella typhimurium LT-2 adenosine diphosphate glucose pyrophosphorylase. J Bacteriol. 1980 Jul;143(1):120–127. doi: 10.1128/jb.143.1.120-127.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. MARTIN R. G., AMES B. N. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J Biol Chem. 1961 May;236:1372–1379. [PubMed] [Google Scholar]
  13. Margoliash E., Nisonoff A., Reichlin M. Immunological activity of cytochrome c. I. Precipitating antibodies to monomeric vertebrate cytochromes c. J Biol Chem. 1970 Mar 10;245(5):931–939. [PubMed] [Google Scholar]
  14. McFadden B. A., Denend A. R. Ribulose diphosphate carboxylase from autotrophic microorganisms. J Bacteriol. 1972 May;110(2):633–642. doi: 10.1128/jb.110.2.633-642.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Murphy T. M., Mills S. E. Immunochemical and enzymatic comparisons of the tryptophan synthase alpha subunits from five species of Enterobacteriaceae. J Bacteriol. 1969 Mar;97(3):1310–1320. doi: 10.1128/jb.97.3.1310-1320.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Parikh I., March S., Cuatercasas P. Topics in the methodology of substitution reactions with agarose. Methods Enzymol. 1974;34:77–102. doi: 10.1016/s0076-6879(74)34009-8. [DOI] [PubMed] [Google Scholar]
  17. Pisano J. J., Bronzert T. J. Analysis of amino acid phenylthiohydantoins by gas chromatography. J Biol Chem. 1969 Oct 25;244(20):5597–5607. [PubMed] [Google Scholar]
  18. Prager E. M., Wilson A. C. The dependence of immunological cross-reactivity upon sequence resemblance among lysozymes. I. Micro-complement fixation studies. J Biol Chem. 1971 Oct 10;246(19):5978–5989. [PubMed] [Google Scholar]
  19. Prager E. M., Wilson A. C. The dependence of immunological cross-reactivity upon sequence resemblance among lysozymes. II. Comparison of precipitin and micro-complement fixation results. J Biol Chem. 1971 Nov 25;246(22):7010–7017. [PubMed] [Google Scholar]
  20. Preiss J. Regulation of adenosine diphosphate glucose pyrophosphorylase. Adv Enzymol Relat Areas Mol Biol. 1978;46:317–381. doi: 10.1002/9780470122914.ch5. [DOI] [PubMed] [Google Scholar]
  21. Rocha V., Crawford I. P., Mills S. E. Comparative immunological and enzymatic study of the tryptophan synthetase beta 2 subunit in the Enterobacteriaceae. J Bacteriol. 1972 Jul;111(1):163–168. doi: 10.1128/jb.111.1.163-168.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Sarich V. M., Wilson A. C. Immunological time scale for hominid evolution. Science. 1967 Dec 1;158(3805):1200–1203. doi: 10.1126/science.158.3805.1200. [DOI] [PubMed] [Google Scholar]
  23. Tarr G. E. Improved manual sequencing methods. Methods Enzymol. 1977;47:335–357. doi: 10.1016/0076-6879(77)47036-8. [DOI] [PubMed] [Google Scholar]
  24. Tronick S. R., Ciardi J. E., Stadtman E. R. Comparative biochemical and immunological studies of bacterial glutamine synthetases. J Bacteriol. 1973 Sep;115(3):858–868. doi: 10.1128/jb.115.3.858-868.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]

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

RESOURCES