Glutathionyl transferase catalyzed addition of glutathione to COMC: A new hypothesis for antitumor activity

被引：31

作者：

Hamilton, DS

Ding, Z

Ganem, B ^{[1
]}

Creighton, DJ

机构：

[1] Univ Maryland, Dept Chem & Biochem, Baltimore, MD 21228 USA

[2] Cornell Univ, Baker Lab, Dept Chem & Chem Biol, Ithaca, NY 14853 USA

来源：

ORGANIC LETTERS | 2002年 / 4卷 / 07期

关键词：

D O I：

10.1021/ol025650h

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

[GRAPHICS] Data are presented indicating that the potent antitumor activity of 2-crotonyloxymethyl-(4R,5R,6R)-4,5,6-trihydroxy-2-cyclohexenone (COTC) and 2-crotonyloxymethyl-2-cyclohexenone (COMC) is not likely the result of glyoxalase I inhibition, as has long been assumed. An alternative hypothesis is presented, based on the finding that COMC is a substrate for human glutathionyl transferase, which produces a transient, highly electrophilic glutathionylated 2-exomethylenecyclohexanone that can covalently modify proteins and nucleic acids.

引用

页码：1209 / 1212

页数：4

共 13 条

[1]

AGHIL O, 1992, ANTI-CANCER DRUG DES, V7, P67

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