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Tritium kinetic isotope effects on enzymatic decomposition of L-tryptophan

Treść / Zawartość
Identyfikatory
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
The tritium kinetic isotope effect on position 2 has been determined in the reaction of decomposition of L-tryptophan, L-Trp, catalyzed by enzyme TPase, (EC 4.1.99.1). The numerical values of isotope effects in the course of reaction were obtained by the competitive method using [1-14C]-L-tryptophan as internal radiometric standard.
Słowa kluczowe
Czasopismo
Rocznik
Strony
17--19
Opis fizyczny
Bibliogr. 13 poz., rys.
Twórcy
autor
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. Boroda E, Kański R, Kańska M (2003) Synthesis of [14C]-L-tryptophan and [14C]-5’-hydroxy-L-tryptophan labeled in the carboxyl group. J Labelled Compd Radiopharm 46:441−447
  • 2. Boroda E, Rakowska S, Kański R, Kańska M (2003)Enzymatic synthesis of L-tryptophan and 5’-hydroxy-Ltryptophan labeled with deuterium and tritium at the alfa-carbon position. J Labelled Compd Radiopharm 46:691−698
  • 3. Cook F (1991) Enzyme mechanism from isotope effects.CRS Press, Boca Raton
  • 4. Isupov MN, Antson AA, Dodson EJ et al. (1998) Crystal structure of tryptophanase. J Mol Biol 276:603−623
  • 5. Kiick DM, Phillips RS (1988) Mechanistic deductions from multiple kinetic and solvent deuterium isotope effects and pH studies of pyrydoxal phosphate dependent carbon-carbon lyases: Escherichia coli tryptophan indolelyase.Biochemistry 27:7339−7344
  • 6. Morino Y, Snell EE (1967) A kinetic study of the reaction mechanism of tryptophanase-catalyzed reaction. J Biol Chem 242:2793−2799
  • 7. Philips RS, Bender SL, Brzovic P, Dunn MF (1990)Mechanism of binding of substrate to tryptophan indolelyase:studies using rapid-scanning and single-wavelength stopped-flow spectrophotometry. Biochemistry 29:8608−8614
  • 8. Philips RS, Demidkina TV, Zakomirdina LN, Bruno S,Ronda L, Mozzarelli A (2002) Crystals of tryptophan indole-lyase and tyrosine phenol-lyase form stable quinonoid complexes. J Biol Chem 277:21592−21597
  • 9. Philips RS, Doshi KJ (1998) Cleavage of Escherichia coli tryptophan indole-lyase by trypsin at Lys406 affects the transmission conformational changes associated with monovalent cation activation. Eur J Biochem 255:508−515
  • 10. Philips RS, Johnson N, Kamath AV (2002) Formation in vitro of hybrid dimers of H463F and Y74F mutant Escherichia coli tryptophan indole-lyase rescues activity with L-tryptophan. Biochemistry 41:4012−4019
  • 11. Philips RS, Lee M (1995) The mechanism of Escherichia coli tryptophan indole-lyase: substituent effects on steadystate and pre-steady-state kinetic parameters for arylsubstituted tryptophan derivatives. Bioorg Med Chem 3:195−205
  • 12. Philips RS, Sundararaju B, Faleev NF (2000) Proton transfer and carbon-carbon bond cleavage in the elimination of indole catalyzed by Escherichia coli tryptophan indole-lyase. J Am Chem Soc 122:1008−1014
  • 13. Tong JY, Yankwich PE (1957) Calculation of experimental isotope effects for pseudo-first order irreversiblereactions. J Phys Chem 61:540−543
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-article-BUJ6-0004-0025
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