<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Fujita S</submitter><funding>Institute for Fermentation Osaka</funding><funding>Ehime University</funding><funding>Japan Society for the Promotion of Science</funding><pagination>107505</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11298593</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>300(8)</volume><pubmed_abstract>Archaeosine (G&lt;sup>+&lt;/sup>) is an archaea-specific tRNA modification synthesized via multiple steps. In the first step, archaeosine tRNA guanine transglucosylase (ArcTGT) exchanges the G15 base in tRNA with 7-cyano-7-deazaguanine (preQ&lt;sub>0&lt;/sub>). In Euryarchaea, preQ&lt;sub>0&lt;/sub>15 in tRNA is further modified by archaeosine synthase (ArcS). Thermococcus kodakarensis ArcS catalyzes a lysine-transfer reaction to produce preQ&lt;sub>0&lt;/sub>-lysine (preQ&lt;sub>0&lt;/sub>-Lys) as an intermediate. The resulting preQ&lt;sub>0&lt;/sub>-Lys15 in tRNA is converted to G&lt;sup>+&lt;/sup>15 by a radical S-adenosyl-L-methionine enzyme for archaeosine formation (RaSEA), which forms a complex with ArcS. Here, we focus on the substrate tRNA recognition mechanism of ArcS. Kinetic parameters of ArcS for lysine and tRNA-preQ&lt;</pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>ArcS from Thermococcus kodakarensis transfers L-lysine to preQ&lt;sub>0&lt;/sub> nucleoside derivatives as minimum substrate RNAs.</pubmed_title><pmcid>PMC11298593</pmcid><funding_grant_id>JP24K09381</funding_grant_id><funding_grant_id>JP20H03211</funding_grant_id><funding_grant_id>G-2022-2-052</funding_grant_id><pubmed_authors>Fujita S</pubmed_authors><pubmed_authors>Yamagami R</pubmed_authors><pubmed_authors>Yokogawa T</pubmed_authors><pubmed_authors>Hirata A</pubmed_authors><pubmed_authors>Oka N</pubmed_authors><pubmed_authors>Hori H</pubmed_authors><pubmed_authors>Kawamura T</pubmed_authors><pubmed_authors>Sugio Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>ArcS from Thermococcus kodakarensis transfers L-lysine to preQ&lt;sub>0&lt;/sub> nucleoside derivatives as minimum substrate RNAs.</name><description>Archaeosine (G&lt;sup>+&lt;/sup>) is an archaea-specific tRNA modification synthesized via multiple steps. In the first step, archaeosine tRNA guanine transglucosylase (ArcTGT) exchanges the G15 base in tRNA with 7-cyano-7-deazaguanine (preQ&lt;sub>0&lt;/sub>). In Euryarchaea, preQ&lt;sub>0&lt;/sub>15 in tRNA is further modified by archaeosine synthase (ArcS). Thermococcus kodakarensis ArcS catalyzes a lysine-transfer reaction to produce preQ&lt;sub>0&lt;/sub>-lysine (preQ&lt;sub>0&lt;/sub>-Lys) as an intermediate. The resulting preQ&lt;sub>0&lt;/sub>-Lys15 in tRNA is converted to G&lt;sup>+&lt;/sup>15 by a radical S-adenosyl-L-methionine enzyme for archaeosine formation (RaSEA), which forms a complex with ArcS. Here, we focus on the substrate tRNA recognition mechanism of ArcS. Kinetic parameters of ArcS for lysine and tRNA-preQ&lt;</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Jun</publication><modification>2025-04-26T05:37:47.724Z</modification><creation>2025-04-06T11:32:39.548Z</creation></dates><accession>S-EPMC11298593</accession><cross_references><pubmed>38944122</pubmed><doi>10.1016/j.jbc.2024.107505</doi></cross_references></HashMap>