<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>9(19)</volume><submitter>Ito T</submitter><pubmed_abstract>&lt;i>Plasmodium&lt;/i> malate-quinone oxidoreductase (MQO) is a membrane flavoprotein catalyzing the oxidation of malate to oxaloacetate and the reduction of quinone to quinol. Recently, using a yeast expression system, we demonstrated that MQO, expressed in place of mitochondrial malate dehydrogenase (MDH), contributes to the TCA cycle and the electron transport chain in mitochondria, making MQO attractive as a promising drug target in &lt;i>Plasmodium&lt;/i> malaria parasites, which lack mitochondrial MDH. However, there is little information on the structure of MQO and its catalytic mechanism, information that will be required to develop novel drugs. Here, we investigated the catalytic site of &lt;i>P. falciparum&lt;/i> MQO (PfMQO) using our yeast expression system. We generated a model structure for Pf</pubmed_abstract><journal>ACS omega</journal><pagination>21647-21657</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11097338</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Insights into the Mechanism of Catalytic Activity of &lt;i>Plasmodium&lt;/i> Parasite Malate-Quinone Oxidoreductase.</pubmed_title><pmcid>PMC11097338</pmcid><pubmed_authors>Nishino K</pubmed_authors><pubmed_authors>Shinohara Y</pubmed_authors><pubmed_authors>Ito T</pubmed_authors><pubmed_authors>Fujii M</pubmed_authors><pubmed_authors>Tojo Y</pubmed_authors><pubmed_authors>Kosako H</pubmed_authors></additional><is_claimable>false</is_claimable><name>Insights into the Mechanism of Catalytic Activity of &lt;i>Plasmodium&lt;/i> Parasite Malate-Quinone Oxidoreductase.</name><description>&lt;i>Plasmodium&lt;/i> malate-quinone oxidoreductase (MQO) is a membrane flavoprotein catalyzing the oxidation of malate to oxaloacetate and the reduction of quinone to quinol. Recently, using a yeast expression system, we demonstrated that MQO, expressed in place of mitochondrial malate dehydrogenase (MDH), contributes to the TCA cycle and the electron transport chain in mitochondria, making MQO attractive as a promising drug target in &lt;i>Plasmodium&lt;/i> malaria parasites, which lack mitochondrial MDH. However, there is little information on the structure of MQO and its catalytic mechanism, information that will be required to develop novel drugs. Here, we investigated the catalytic site of &lt;i>P. falciparum&lt;/i> MQO (PfMQO) using our yeast expression system. We generated a model structure for Pf</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 May</publication><modification>2026-06-02T21:23:27.619Z</modification><creation>2026-04-20T03:14:20.564Z</creation></dates><accession>S-EPMC11097338</accession><cross_references><pubmed>38764661</pubmed><doi>10.1021/acsomega.4c02614</doi></cross_references></HashMap>