Drug target validation of the trypanothione pathway enzymes through metabolic modelling
Version of Record online: 4 APR 2012
© 2012 The Authors Journal compilation © 2012 FEBS
The FEBS Journal
Volume 279, Issue 10, pages 1811–1833, May 2012
How to Cite
Olin-Sandoval, V., González-Chávez, Z., Berzunza-Cruz, M., Martínez, I., Jasso-Chávez, R., Becker, I., Espinoza, B., Moreno-Sánchez, R. and Saavedra, E. (2012), Drug target validation of the trypanothione pathway enzymes through metabolic modelling. The FEBS Journal, 279: 1811–1833. doi: 10.1111/j.1742-4658.2012.08557.x
- Issue online: 23 APR 2012
- Version of Record online: 4 APR 2012
- Accepted manuscript online: 6 MAR 2012 02:53PM EST
- (Received 12 July 2011, revised 13 February 2012, accepted 1 March 2012)
Fig. S1. SDS–PAGE of the purified enzymes.
Fig. S2. Kinetics of TcTryS against GSH.
Fig. S3. γECS inhibition by GSH and γEC.
Fig. S4. Dependence of flux and T(SH)2 concentration on the k values of the leaks.
Table S1. Comparison of the kinetic parameters of the pathway enzymes with those reported in the literature.
Table S2. Determination of GS and TryS activities in parasite extracts.
Table S3. Enzyme activities in parasite extracts exposed to various conditions.
Table S4. Thiol content in various strains of Trypanosoma cruzi epimastigotes.
Table S5. Reactions as written in GEPASI/COPASI.
Table S6. Summary of the rate constant values used in the model.
Table S7. Summary of the affinity values used for each enzyme.
Table S8. Robustness of the model.
Table S9. Elasticity coefficients.
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