Enzyme chemistry of dithiohemiacetals: synthesis and characterization of S-D-dithiomandeloylglutathione as an alternate substrate for glyoxalase I.
Enzyme chemistry of dithiohemiacetals: synthesis and characterization of S-D-dithiomandeloylglutathione as an alternate substrate for glyoxalase I.
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二硫半缩醛的酶化学：作为乙二醛酶 I 替代底物的 S-D-二硫扁桃酰谷胱甘肽的合成和表征。
DOI：
10.1016/0006-291x(91)91241-4
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发表时间：
1991
影响因子：
3.1
通讯作者：
Creighton,DJ
中科院分区：
文献类型：
--
作者：
Li,J;Guha,MK;Creighton,DJ
通过GSH与S-羧甲基（D，L）-二硫代扁桃酸酯的二硫代酯交换反应，合成了D-和L-型S-二硫代扁桃酰谷胱甘肽（1）。动力学和产物分析研究表明，酵母glycoprotein酶I有效地催化D-1立体选择性转化为GSH-苯基乙二醛二硫代半缩醛（2），分离为2和第二个GSH分子之间的二硫化物加合物。这一观察结果表明，二硫代酯底物类似物一般应作为涉及硫代半缩醛中间体的酶催化反应的机理探针。
Both the D-and L-forms of S-dithio mandeloylglutathione (1) have been synthesized by a dithio ester-interchange reaction between GSH and S-carboxymethyl (D, L)-dithio mandelate. Kinetic and product analysis studies indicate that yeast glyoxalase I efficiently catalyzes the stereoselective conversion of D-1 to GSH-phenylglyoxal dithio hemiacetal (2), isolated as a disulfide adduct between 2 and a second molecule of GSH. This observation suggests that dithio ester substrate analogues should be generally useful as mechanistic probes of enzyme catalyzed reactions involving thiohemiacetal intermediates.