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结构洞察 Old Yellow Enzyme 从克氏锥虫立体选择性产生 PGF2α。

Structural insight into the stereoselective production of PGF2α by Old Yellow Enzyme from Trypanosoma cruzi.

机构信息

Department of Applied Chemistry, Graduate School of Engineering, Osaka University, Yamada-Oka, Suita, Japan.

出版信息

J Biochem. 2011 Nov;150(5):563-8. doi: 10.1093/jb/mvr096. Epub 2011 Aug 12.

DOI:10.1093/jb/mvr096
PMID:21840922
Abstract

Old yellow enzyme (OYE) is an NADPH oxidoreductase capable of reducing a variety of compounds. It contains flavin mononucleotide (FMN) as a prosthetic group. A ternary complex structure of OYE from Trypanosoma cruzi (TcOYE) with FMN and one of the substrates, p-hydroxybenzaldehyde, shows a striking movement around the active site upon binding of the substrate. From a structural comparison of other OYE complexed with 12-oxophytodienoate, we have constructed a complex structure with another substrate, prostaglandin H(2) (PGH(2)), to provide a proposed stereoselective reaction mechanism for the reduction of PGH(2) to prostaglandin F(2α) by TcOYE.

摘要

老黄酶(OYE)是一种 NADPH 氧化还原酶,能够还原多种化合物。它含有黄素单核苷酸(FMN)作为辅基。来自克氏锥虫(TcOYE)的 OYE 与 FMN 和一种底物对羟基苯甲醛的三元复合物结构显示,在结合底物时,活性位点周围会发生显著的运动。通过与其他 OYE 与 12-氧代植二烯酸复合物的结构比较,我们构建了与另一种底物前列腺素 H2(PGH2)的复合物结构,为 TcOYE 将 PGH2 还原为前列腺素 F2α 的立体选择性反应机制提供了一个建议。

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