A Covalent Succinylcysteine-like Intermediate in the Enzyme-Catalyzed Transformation of Maleate to Fumarate by Maleate Isomerase
A Covalent Succinylcysteine-like Intermediate in the Enzyme-Catalyzed Transformation of Maleate to Fumarate by Maleate Isomerase
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DOI：
10.1021/ja1053576
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发表时间：
2010-08-25
影响因子：
15
通讯作者：
Grogan, Gideon
中科院分区：
文献类型：
--
作者：
Fisch, Florian;Fleites, Carlos Martinez;Grogan, Gideon
马来酸异构酶（maleanoisomerase，MI）是天冬氨酸/谷氨酸消旋酶超家族的成员，催化顺反异构化马来酸酯中的C2-C3双键生成富马酸酯。突变的研究，结合与马来酸盐共结晶的诺卡氏菌MI的C194 A突变体的结构，揭示了一个前所未有的模式的超家族的催化，其中异构化反应是由亲核攻击的半胱氨酸在双键，产生共价琥珀酰半胱氨酸样中间体。
Maleate isomerase (MI), a member of the Asp/Glu racemase superfamily, catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. Mutational studies, in conjunction with the structure of the C194A mutant of Nocardia farcinica MI cocrystallized with maleate, have revealed an unprecedented mode of catalysis for the superfamily in which the isomerization reaction is initiated by nucleophilic attack of cysteine at the double bond, yielding a covalent succinylcysteine-like intermediate.