Glutathione transferases from parasites: A biochemical view

被引：75
|
作者：
Torres-Rivera, Anayetzin [1 ]
Landa, Abraham [1 ]
机构：
[1] Univ Nacl Autonoma Mexico, Fac Med, Dept Microbiol & Parasitol, Mexico City 04510, DF, Mexico
来源：
ACTA TROPICA | 2008年 / 105卷 / 02期
关键词：
parasites; GST; substrate specificity; kinetics; crystals; drug-design;
D O I：
10.1016/j.actatropica.2007.08.005
中图分类号：
R38 [医学寄生虫学]; Q [生物科学];
学科分类号：
07 ; 0710 ; 09 ; 100103 ;
摘要：
The glutathione transferase (GST) system of parasites represents the main detoxification mechanism of hydrophobic and electrophilic compounds. Parasites lack the CYP450 activity, hence part of its function has been taken over by other enzymes including GSTs. Cytosolic GSTs (cGSTs) are found in this system and constitute a versatile and numerous group that in parasites display many peculiarities in contrast to mammalian cGSTs. This review summarizes aspects of the biochemistry of parasite cGSTs such as substrate specificities, inhibitor sensitivities, classification, kinetics and catalysis, as well as some aspects of their protective role. (C) 2007 Elsevier B.V. All rights reserved.
引用
收藏
页码：99 / 112
页数：14
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