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Tytuł artykułu

Funkcja dekarboksylazy lizynowej w regulacji biosyntezy alkaloidow chinolizydynowych

Treść / Zawartość

Warianty tytułu

Języki publikacji

PL

Abstrakty

EN
Lysine decarboxylase is a key enzyme of quinolizidine alkaloids biosynthesis. These alkaloids are characterized by either the properties of antinutritive food components and those of common drugs. The concentration of alkaloids in plants depends on biotic and abiotic stress. Alkaloids are often considered as a plant's "chemical weapon".

Wydawca

-

Rocznik

Tom

47

Numer

6

Opis fizyczny

s.57-68,rys.,tab.,bibliogr.

Twórcy

autor
  • Instytut Chemii Bioorganicznej PAN, ul.Noskowskiego 12/14, 61-704 Poznan

Bibliografia

  • [1] Astriab M. 1998. Nucleic Acids and their Constituents. (Abstract). Scientific Publishers OWN, Poznań: 35, 103.
  • [2] Astriab M. 1996. Izolacja, oczyszczanie i właściwości dekarboksylazy lizynowej (LDC) z łubinu (Lupinus luteus i Lupinus albus). W: Frencel I., Gulewicz K. (red.) Łubin: kierunki badań i perspektywy użytkowe. Polskie Towarzystwo Łubinowe i Instytut Chemii Bioorganicznej PAN, Poznań: 204-211.
  • [3] Borrell A., Culianez-Macia F., Altabella T., Besford R., Flores D., Tiburcio A. F. 1995. Arginine decarboxylase is localized in chloroplasts. Plant Physiol. 109: 771-776.
  • [4] Cairo G., Tacchini L., Pogliaghi G., Anzon E., Tomasi A., Bernelli-Zazzera A. 1995. Induction of ferritin synthesis by oxidative stress. J. Biol. Chem. 2: 700-703.
  • [5] Fecker L. F., Rugenhagen C., Berlin J. 1993. Increased production of cadaverine and anabasine in hairy root cultures of Nicotina tabacum expressing a bacterial lysine decarboxylase gene. Plant Molecular Biology 23: 11-21.
  • [6] Fecker L., Beier H., Berlin J. 1986. Cloning and characterisation of a lysine decarboxylase gene from Hafnia alvei. Mol. Gen. Genet. 203: 177-184.
  • [7] Harborne J. B. 1982. Introduction to ecological biochemistry. Academic Press, London, New York.
  • [8] Hemila H. 1991. Sequence of a PAL-related lipoprotein from Bacillus subtilis. FEMS Microbiol. Lett. 66: 37-41.
  • [9] Herminghaus S., Schreier P. H., McCarthy J., Landsmann J., Botterman J., Berlin J. 1991. Expression of bacterial lysine decarboxylase gene and transport of the protein into chloroplasts of transgenic tobacco. Plant Molecular Biology 17: 475-486.
  • [10] Herminghaus S., Tholl D., Rugenhagen C., Fecker L. F., Leuschner C., Berlin J. 1996. Improved metabolic action of a bacterial lysine decarboxylase gene in tobacco hairy root cultures by its fusion to a rbcS transit peptide coding sequence. Transgenic Research 5: 193-201.
  • [11] Kikuchi Y., KojimaH., Tanaka T., Takatsuka Y., Kamio Y. 1997. Characterization of asecond lysine decarboxylase isolated from Escherichia coli. J. Bacteriol. 179: 4486-4492.
  • [12] Kutchen T. M. 1995. The Basis for Metabolic Engineering of Medical Plants. The Plant Cell 7: 1059-1070.
  • [13] Lemonnier M., Lane D. 1998. Expression of the second lysine decarboxylase gene of Escherichia coli. Microbiology 144: 751-760.
  • [14] Leveque F., Gazeau M., Fromant M., Blanquet S., Plateau P. 1991. Control of Escherichia coli lytyl-tRNA synthetase expression by anaerobiosis. J. Bacteriol. 173: 7903-7910.
  • [15] Maurelli A. T., Fernandez R. E., Bloch C. A., Rode C. K., Fasano A. 1998. ,,Black holes" and bacterial pathogenicity: a large genomic deletion that enhances the virulence of Shigella sp. and enteroinvasive Escherichia coli. PNAS 95: 3943-3948.
  • [16] Munro H. N., Linder M. C. 1978. Ferritin: structure, biosynthesis and role in iron metabolism. Physiol. Rev. 2: 317-396.
  • [17] Park Y. K., Bearson B., Bang S. H., Bang I. S., Foster J. W. 1996. Internal pH crisis, lysine decarboxylase and the acid tolerance response of Salmonella typhimurium. Molecular Microbiology 20: 605-611.
  • [18] Rhodes M. J. C. 1994. Physiological role for secondary metabolites in plants: some progress, many outstanding problems. Plant Molecular Biology 24: 1-20.
  • [19] Rowbury R. J. 1997. Regulatory components, including integration host factor, CysB and H-NS, that influence pH responses in Escherichia coli. Lett. in App. Microbiol. 24: 319-328.
  • [20] Schoofs G., Teichmann S., Hartmann T., Wink M. 1983. Lysine decarboxylase in plants and its integration in quinolizidine alkaloid biosynthesis. Phytochem. 22: 65-69.
  • [21] Scinto L., Daffner K., Dressler D., Ransil B. I., Rentz D., Weintraub S., Mesulam M., Potter H. 1994. A potential noninvasive neurobiological test for Alzheimer's disease. Science 266: 1051-1054.
  • [22] Shi X., Bennett G. N. 1995. Effects of multicopy LeuO on the expression of the acid-inducible lysine decarboxylase gene in Escherichia coli. J. Bacteriol. 177: 810-814.
  • [23] Shi X., Hirshfield I. N. 1996. The survival benefit of short-chain organic acids and the inducible arginine and lysine decarboxylase genes for Escherichia coli. Lett. in App. Microbiol. 22: 393-396.
  • [24] Smól J., Twardowski T. 1998. Ferrytyna - specyficzne białko ochronne. Podstawy Biologii Komórki 25: 511-524.
  • [25] Southon I., Buckingham J. 1989. Dictionary of alkaloids. Chapman and Hall, London.
  • [26] Tyler V. E. 1994. Herbs of choice. Haworth Press, New York.
  • [27] Wink M. 1987. Alkaloids: Biochemistry, Metabolism, and Function in Plants and Cell Suspension Cultures. Planta medica 53: 509-514.
  • [28] Wink M., Hartmann T. 1981. Sites of enzymatic synthesis of quinolizidine alkaloids and their accumulation in Lupinus polyphyllus Z. Pfanzenphysiol. Bd. 102: 337-344.
  • [29] Wink M., Hartmann T. 1979. Cadaverine-pyruvate transamination: the principal step of enzymatic quinolizidine alkaloid biosynthesis in Lupinus polyphyllus cell suspension cultures. FEBS Letters 101: 343-346.
  • [30] Wink M., Hartmann T. 1982. Localization of the enzymes of quinolizidine alkaloid biosynthesis in leaf chloroplasts of Lupinus polyphyllus. Plant Physiology 70: 74-77.
  • [31] Wink M., Hartmann T., Schiebel H. M. 1979. A model mechanism for the enzymatic synthesis of lupin alkaloids Z. Naturforsch. 34c: 704-708.
  • [32] Wink M., Twardowski T. 1992. Allelochemical properties of alkaloids. Effects on plants, bacteria and protein biosynthesis. Allelopathy: Basic and applied aspects. Chapman and Hall, London: 129-150.
  • [33] Yamamoto Y., Miwa Y., Miyoshi K., Furuyama J., Ohmori H. 1997. The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme. Genes and Genetic Systems 72: 167-172.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

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