TY - JOUR
T1 - Dissecting the catalytic mechanism of Trypanosoma brucei trypanothione synthetase by kinetic analysis and computational modelling.
AU - Leroux, A.E.
AU - Haanstra, J.R.
AU - Bakker, B.M.
AU - Krauth-Siegel, R.L.
PY - 2013
Y1 - 2013
N2 - Background: Trypanothione synthetase catalyzes the conjugation of spermidine with two GSH molecules to form trypanothione. Results: The kinetic parameters were measured under in vivo-like conditions. A mathematical model was developed describing the entire kinetic profile. Conclusion: Trypanothione synthetase is affected by substrate and product inhibition. Significance: The combined kinetic and modeling approaches provided a so far unprecedented insight in the mechanism of this parasite-specific enzyme. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
AB - Background: Trypanothione synthetase catalyzes the conjugation of spermidine with two GSH molecules to form trypanothione. Results: The kinetic parameters were measured under in vivo-like conditions. A mathematical model was developed describing the entire kinetic profile. Conclusion: Trypanothione synthetase is affected by substrate and product inhibition. Significance: The combined kinetic and modeling approaches provided a so far unprecedented insight in the mechanism of this parasite-specific enzyme. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
UR - https://www.scopus.com/pages/publications/84882298171
UR - https://www.scopus.com/inward/citedby.url?scp=84882298171&partnerID=8YFLogxK
U2 - 10.1074/jbc.M113.483289
DO - 10.1074/jbc.M113.483289
M3 - Article
SN - 0021-9258
VL - 288
SP - 23751
EP - 23764
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
ER -