Title : Differential catalytic efficiency of allelic variants of human glutathione S-transferase Pi in catalyzing the glutathione conjugation of thiotepa.

Pub. Date : 1999 Jun 1

PMID : 10334868






4 Functional Relationships(s)
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1 Increased glutathione (GSH) conjugation through catalysis by GSH S-transferases (GSTs) is believed to be an important mechanism in tumor cell resistance to alkylating agents. Glutathione glutathione S-transferase pi 1 Homo sapiens
2 Increased glutathione (GSH) conjugation through catalysis by GSH S-transferases (GSTs) is believed to be an important mechanism in tumor cell resistance to alkylating agents. Glutathione glutathione S-transferase pi 1 Homo sapiens
3 In the present study, we report that the allelic variants of human Pi class GST (hGSTP1-1), which differ in their primary structures at amino acids in positions 104 and/or 113, exhibit significant differences in their activity in the GSH conjugation of alkylating anticancer drug thiotepa. Glutathione glutathione S-transferase pi 1 Homo sapiens
4 The hGSTP1-1-catalyzed GSH conjugation of thiotepa was time and protein dependent and followed Michaelis-Menten kinetics. Glutathione glutathione S-transferase pi 1 Homo sapiens