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Carbon isotope effects in the studies of the mechanism of action of tyrosine phenol-lyase

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Warianty tytułu
Konferencja
Proceedings of the IV All-Polish Conference on Radiochemistry and Nuclear Chemistry9-11 May 2005, Kraków-Przegorzały, Poland
Języki publikacji
EN
Abstrakty
EN
12C/14C kinetic isotope effects on the hydrolytic cleavage of tyrosine to phenol and ammonium pyruvate catalyzed by Citrobacter freundii tyrosine phenol-lyase have been determined in positions 2, 3 and ring-1' of L-tyrosine. The competitive method with dual-label approach was applied with 3',5'-ring 3H as remote label. The results revealed the change of the effect on carbon atom in position 2 during the reaction course from the high normal values to low inverse values. On the other hand, the effect values on 3 and ring-1' position remained constant during the reaction course. The discussion of these results regarding the reaction mechanism is presented.
Czasopismo
Rocznik
Strony
7--11
Opis fizyczny
Bibliogr. 11 poz., rys.
Twórcy
autor
autor
  • Department of Chemistry, University of Warsaw, 1 Pasteura Str., 02-093 Warsaw, Poland, Tel.: +48 22 822 02 11 ext. 509, Fax: +48 22 822 59 96,, mkanska@alfa.chem.edu.pl
Bibliografia
  • 1. Augustyniak W, Kański R, Kańska M (2001) Synthesis of carbon-14 labeled [1-14C]-, and [2-14C]-L-tyrosine. J Labelled Compd Radiopharm 44:553−560
  • 2. Augustyniak W, Suchecki P, Kański, R, Kańska M (2004)Syntheses of carbon and hydrogen isotopomers of L-tyrosine. Synth Appl Isot Labelled Compd, Wiley & Sons, Chichester, UK 8:235−238
  • 3. Axelsson BS, Bjurling P, Matsson O, Langstrom B (1992)11C/14C kinetic isotope effects in enzyme mechanism studies. 11C/14C kinetic isotope effect of the tyrosine phenol-lyase catalyzed alfa, beta-elimination of L-tyrosine.J Am Chem Soc 114:1502−1503
  • 4. Faleev NG, Ruvinov SB, Demidkina TV et al. (1988)Tyrosine phenol-lyase from Citrobacter intermedius.Factors controlling substrate specificity. Eur J Biochem 177:395−401
  • 5. Kański R, Augustyniak W, Kańska M (2006) Synthesis of ring labeled [1’-14C]-L-tyrosine. Nukleonika 51;Suppl 2:s13−s16
  • 6. Kumagai H, Kashima N, Yamada H (1970) Racemization of D or L-alanine by crystalline tyrosine phenol-lyase from Escherichia intermedia. Biochem Biophys Res Commun 39:796−801
  • 7. Kumagai H, Yamada H, Matsui H, Ohkishi H, Ogata K (1970) Tyrosine phenol-lyase. I. Purification, crystallization,and properties. J Biol Chem 245:1767−1772
  • 8. Lipiński R, Augustyniak W, Kański R, Kańska M (2003)Kinetic isotope effects in the studies of the mechanism of action of L-tyrosine phenol lyase. Ann Pol Chem Soc 2:3−5
  • 9. Phillips RS, Demidkina TV, Faleev NG (2003) Structure and mechanism of tryptophan indole-lyase and tyrosine phenol-lyase. Biochem Biophys Acta 1647:167−172
  • 10. Tong JT, Yankwich PE (1964) Calculation of experimental isotope effects for pseudo first-order irreversible reactions. J Phys Chem 61:540−543
  • 11. Yamada H, Kumagai H (1975) Synthesis of L-tyrosinerelated amino acids by β-tyrosinase. Adv Appl Microbiol 19:249−288
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-article-BUJ6-0004-0023
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