Shikimate pathway in yeast cels: enzymes, functioning, regulation - a review

• Autorzy: Gientka I. , Duszkiewicz-Reinhard W.
• Języki publikacji: EN

Abstrakty

EN

The shikimic acid pathway occurs in various groups of microorganisms, plants and parasites, while it does not occur in animal organisms. An interesting protein synthesized by the yeast is the product of ARO1 gene known as AROM protein. The occurrence of AROM protein in cells of the yeast is the most important difference as compared to the functioning of the shikimate pathway in other organisms. The shikimate pathway constitutes a good source for designing antimicrobial agents. The key industrial significance of shikimic acid pathway metabolites consists in shikimic acid application as a starter material for the synthesis of a neuraminidase inhibitor (GS4104) and agents used in the antitumor therapy. The knowledge on that pathway should be continuously extended in the aspect of potential acquisition of its metabolites.

• Wydawca: -
• Czasopismo: Polish Journal of Food and Nutrition Sciences
• Rocznik: 2009
• Tom: 59
• Numer: 2
• Opis fizyczny: p.113-118,fig.,ref.

Twórcy

autor

Gientka I.

• Department of Biotechnology, Microbiology and Food Evaluation, Warsaw University of Life Sciences, Nowoursynowska 166, 02-776 Warsaw, Poland

autor

Duszkiewicz-Reinhard W.

Bibliografia

• 1. Amrhein N., Johanning J., Schab J.J., Schulz A., Biochemical basis for glyphosate tolerance in a bacterium and plant tissue culture. FEBS Lett., 1983,157, 191–195.
• 2. Arndt K., Fink G.R., GCN4 protein. A positive transcription factor in yeast, binds general control promoters at all 5’-TGACTC-3’ sequences. Proc. Antl. Acad. Sci. Biochem., 1986, 83, 8516–‑8520.
• 3. Bender S.L., Widlanski T., Knowles J.R., Dehydroquinate synthase: the use of substrate analogues to probe the early steps of catalyzed reaction. Biochemistry, 1998, 28, 7560–7572.
• 4. Bode R., Melo C., Birnbaum D., Mode of action of glyphosate in Candida maltosa. FEMS Microbiol. Lett., 1984, 140, 83–85.
• 5. Bode R., Schauer F., Birnbaum D., Comparative studies on the enzymological basis for growth inhibition by glyphosate in some yeast species. Biochem. Physiol. Pflanzen, 1986, 181, 39–46.
• 6. Boocock M.R., Coggins J.R., Kinetics of EPSP synthase inhibition by glyphosate. FEBS Lett., 1983, 154, 127–133.
• 7. Bornemann S., Ramjee M.K., Balasubramanian S., Abell C., Coggins J.R., Lowe D.J., Thorneley R.N., Escherichia coli chorismate synthase catalyses the conversion of (6S)-6-fluoro-5-EPSP-3-P to 6-fluorochorismate. Implication for the enzyme mechanism and the antimicrobial action of (6S)-6-fluoroshikimate. J. Biol. Chem., 1995, 270, 22811–22815.
• 8. Braus G.H., Aromatic amino acid biosynthesis in the yeast Saccharomyces cerevisiae: a model system for the regulation of an eukaryotic biosynthetic pathway. Microb. Rev., 1991, 55, 349–370.
• 9. Bulloch E.M., Jones M.A., Parker E.J., Osborne A.P., Stephens E., Davies G.M., Coggins J.R., Abell C., Identification of 4-amino‑4- deoxychorismate synthase as the molecular target for the antimicrobial action of (6S)-6-fluoroshikimate. J. Am. Chem. Soc., 2004, 126, 9912–9913.
• 10. Campbell S.A., Richards T.A., Mui E.J., Samuel B.U., Coggins J.R., McLeod R., Roberts C.W., A complete shikimate pathways in Toxoplasma gondii: an ancient eukaryotic innovation. Int. J. Parasitol., 2004, 34, 5–13
• 11. Davies G.M., Barrett-Bee K.J., Jude D.A., Lehan M., Nichols W.W., Pinder P.E., Thain J.L., Watkins W.J., Wilson R.G., (6S)- 6-fluoroshikimic acid, an antibacterial agent acting on aromatic biosynthesis pathway. Antimicrob. Agents Chemother., 1994, 38, 403–406.
• 12. Duncan K., Edwards R.M., Coggins J.R., The pentafunctional arom enzyme of Saccharomyces cerevisiae is a mosaic of monofunctional domains. Biochem. J., 1987, 246, 375–86.
• 13. Duncan K., Edwards R.M., Coggins J.R., The Saccharomyces cerevisiae ARO1 gene. An example of the co-ordinate regulation of five enzymes on a single biosynthetic pathway. FEBS Lett., 1988, 241, 83–88.
• 14. Fisher R.S., Rubin J.L., Glyphosate sensitivity of 5-enolpyruvylshikimate- 3-phosphate synthase from Bacillus subtilis depends upon state of activation induced by monovalent cations. Arch. Biochem. Biophys., 1987, 256, 325–334.
• 15. Floss H.G., Onderka D.K., Carroll M., Stereochemistry of the 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase reaction and the chorismate synthase reaction. J. Biol. Chem., 1972, 247,736–744.
• 16. Gientka I., The influence of p-aminobenzoic acid on yeast cell metabolism. 2007, Doctoral Thesis, Warsaw University of Agriculture, Poland, pp. 69–78 (in Polish).
• 17. Graham L.D., Gillies F.M., Coggins J.R., Over-expression of the yeast multifunctional arom protein. Biochim. Biophys. Acta, 1993, 1216, 417–424.
• 18. Hartmann M., Schneider T.R., Pfeil A., Heinrich G., Lipscomb W.N., Braus G.H., Evolution of feedback-inhibited beta/alpha barrel isoenzymes by gene duplication and a single mutation, Proc. Natl. Acad. Sci. USA, 2003, 100, 862–867.
• 19. Helmstaedt K., Strittmatter A., Lipscomb W.N., Braus G.H. Evolution of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase-encoding genes in the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA, 2005, 102, 9784–9789.
• 20. Herrmann K.M., The shikimate pathway as an entry to aromatic secondary metabolism. Plant Physiol., 1995, 107, 7–12.
• 21. Herrmann K.M., Weaver I., The shikimate pathway. Annu. Rev. Plant Physiol. Plant. Mol. Biol., 1999, 50, 473–503.
• 22. Hinnebusch A.G. Natarajan K., Gcn4p, a master regulator of gene expression is controlled at multiple levels by diverse signals of starvation and stress. Eukaryot. Cell, 2002, 1, 22–32.
• 23. Hinnebusch A.G., Mechanism of gene regulation in the general control of amino acid biosynthesis in Saccharomyces cerevisiae. Microb. Rev., 1988, 52, 248–273.
• 24. Jiang S., Singh G., Chemical synthesis of shikimic acid and its analogues. Tetrahedron, 1998, 54, 4697–4753.
• 25. Karpf M., Trussardi R., New, azid-free transformation of epoxides into 1,2-diamino compounds: synthesis of the anti-influenza neuraminidase inhibitor oseltamivir phosphate (Tamiflu). J. Org. Chem., 2001, 66, 2044–2051.
• 26. Krämer M., Bongaerts J., Bovenberg R., Kremer S., Müller U., Orf S., Wubbolts M., Raeven L., Metabolic engineering for microbial production of shikimic acid. Metab. Eng., 2003, 5, 277–283.
• 27. Künzler M.G., Paravicini G., Egli Ch.M., Irniger S., Braus G.H., Cloning, primary structure and regulation of the ARO4 gene, encoding the tyrosine-inhibited 3-deoxy-D-arabinoheptulosonate‑7- phosphate synthase from Saccharomyces cerevisiae. Gene, 1992, 113, 67–74.
• 28. Meganathan R., Ubiquinone biosynthesis in microorganisms. FEMS Microb. Lett., 2001, 203, 131–139.
• 29. Paravicini G., Mösch H-U., Schmidheini T., Braus G., The general control activator protein GCN4 is essential for a basal level of ARO3 gene expression in Saccharomyces cervisiae. Mol. Cell Biol., 1989, 9, 144–151.
• 30. Pilch P.F., Somerville R.L., Fluorine-containing analogues of intermediatesin the shikimate pathway. Biochemistry, 1976, 15, 5315–5320.
• 31. Quevillon-Cheruel S., Leulliot N., Meyer P., Graille M., Bremang M., Blondeau K., Sorel I., Poupon A., Janin J., van Tilbeurgh H., Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae. J. Biol. Chem., 2004, 279, 619–625.
• 32. Ramjee M., Balsubramanian S., Reaction of (6R)-6-F-EPSP with recombinant Escherichia coli chorismate synthase generates a stable flavin mononucleotide semiquinone radical. J. Am. Chem. Soc., 1992, 114, 3151–3153.
• 33. Reed L.J., Schram A.C., Loveless L.E., Inhibition of Saccharomyces cerevisiae by p-aminobenzoic acid and its reversal by the aromatic amino acids. J. Biol. Chem., 1959, 234, 909–911.
• 34. Roberts C.W., Roberts F., Lyons R.E., Kiristis M.J., Mui E.J., Finnerty J., Johnson, J.J., Ferguso, J.P., Coggins J.R., Krell T., Coombs G.H., Milhous W.K., Kyle D.E., Tzipori S., Barnwell J., Dame J.B., Carlton J., McLeod R., The shikimate pathway and its branches in apicomplexan parasites. J. Infect. Diseases, 2002, 185, 25–36.
• 35. Schnappauf G., Hartmann M. Künzler M.G., Braus G.H., The two 3-deoxy-D-arabinoheptulosonate-7-phosphate synthase isoenzymes from Saccharomyces cerevisiae show different kinetic models of inhibition. Arch. Microbiol., 1998, 169, 517–524.
• 36. Steinrucken H.C., Amrhein N., 5-enolpyruvylshikimate-3‑phosphate synthase of Klebsiella pneumoniae. Inhibition by glyphosate [N-(phosphomethyl)glycine]. Eur. J. Biochem., 1984, 143, 351–357.
• 37. Stryer L., Biochemia. 1997,Wydawnictwo Naukowe PWN, Warszawa (in Polish).
• 38. Surovtseva E.G., Accumulation of shikimic acid by the yeast in the presence of p-aminobenzoic acid. Mikrobiologija, 1970, 6, 39, 996–1000.
• 39. Teshiba S., Furter R., Niederberger P., Braus G., Paravicini G., Hutter R., Cloning of ARO3 gene of Saccharomyces cerevisiae and its regulation. Mol. Gen. Genet., 1986, 205, 353–357.
• 40. Widlanski T., Bender S.L., Knowles J.R. Dehydroquinate synthase: the use of substrate analogues to probe the late steps of catalyzed reaction. Biochemistry, 1989, 28, 7572–7582.
• 41. Zhang Y., Liu A., Ye Z.G., Lin J., Xu L.Z., Yang S.L., New approach to the total synthesis of (-)-zeylenone from shikimic acid. Chem. Pharm. Bull. (Tokyo), 2006, 54, 1459–1461.

Uwagi

PL

Rekord w opracowaniu