恶性疟原虫乳清苷5'-单磷酸脱羧酶催化乳清苷5'-单磷酸（OMP）脱羧反应的结构基础。
Structural basis for the decarboxylation of orotidine 5'-monophosphate (OMP) by Plasmodium falciparum OMP decarboxylase.
作者信息
Tokuoka Keiji, Kusakari Yukiko, Krungkrai Sudaratana R, Matsumura Hiroyoshi, Kai Yasushi, Krungkrai Jerapan, Horii Toshihiro, Inoue Tsuyoshi
机构信息
Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
出版信息
J Biochem. 2008 Jan;143(1):69-78. doi: 10.1093/jb/mvm193. Epub 2007 Nov 1.
Orotidine 5'-monophoshate decarboxylase (OMPDC) catalyses the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). Here, we report the X-ray analysis of apo, substrate or product-complex forms of OMPDC from Plasmodium falciparum (PfOMPDC) at 2.7, 2.65 and 2.65 A, respectively. The structural analysis provides the substrate recognition mechanism with dynamic structural changes, as well as the rearrangement of the hydrogen bond array at the active site. The structural basis of substrate or product binding to PfOMPDC will help to uncover the decarboxylation mechanism and facilitate structure-based optimization of antimalarial drugs.
乳清苷5'-单磷酸脱羧酶（OMPDC）催化乳清苷5'-单磷酸（OMP）脱羧生成尿苷5'-单磷酸（UMP）。在此，我们分别报道了恶性疟原虫（PfOMPDC）的无配体、底物或产物复合物形式的X射线分析结果，分辨率分别为2.7 Å、2.65 Å和2.65 Å。结构分析揭示了底物识别机制以及活性位点氢键阵列的重排，这些都伴随着动态结构变化。底物或产物与PfOMPDC结合的结构基础将有助于揭示脱羧机制，并促进基于结构的抗疟药物优化。
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