<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kim S</submitter><funding>MCIN/AEI/10.13039/501100011033, ESF Investing in your future</funding><funding>National Research Foundation of Korea</funding><pagination>120</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12096693</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>24(1)</volume><pubmed_abstract>&lt;h4>Background&lt;/h4>Cadaverine, displaying potential in medicine, agriculture and polyamide production, is biologically produced through L-lysine decarboxylation. Considering the potential of the polyamide market, its biological production has been focused on with following diverse efforts to improve the production. In Escherichia coli, lysine decarboxylase exists in two forms: CadA and LdcC, and it is known that CadA exhibits superior catalytic activity compared to LdcC. Despite its potential, cadaverine production is limited due to increased intracellular pH, which destabilizes the decameric structure of CadA and inhibits its activity.&lt;h4>Results&lt;/h4>In this study, based on the structural analysis, a chimeric CadA enzyme, CL2, was engineered by replacing its pH-sensitive region with a str</pubmed_abstract><journal>Microbial cell factories</journal><pubmed_title>Region-based segmental swapping of homologous enzymes for higher cadaverine production.</pubmed_title><pmcid>PMC12096693</pmcid><funding_grant_id>RYC2020-028880-I</funding_grant_id><funding_grant_id>RS-2024-00400033</funding_grant_id><pubmed_authors>Kim S</pubmed_authors><pubmed_authors>Noh MH</pubmed_authors><pubmed_authors>Lim HG</pubmed_authors><pubmed_authors>Yang JS</pubmed_authors><pubmed_authors>Ye DY</pubmed_authors><pubmed_authors>Jung GY</pubmed_authors></additional><is_claimable>false</is_claimable><name>Region-based segmental swapping of homologous enzymes for higher cadaverine production.</name><description>&lt;h4>Background&lt;/h4>Cadaverine, displaying potential in medicine, agriculture and polyamide production, is biologically produced through L-lysine decarboxylation. Considering the potential of the polyamide market, its biological production has been focused on with following diverse efforts to improve the production. In Escherichia coli, lysine decarboxylase exists in two forms: CadA and LdcC, and it is known that CadA exhibits superior catalytic activity compared to LdcC. Despite its potential, cadaverine production is limited due to increased intracellular pH, which destabilizes the decameric structure of CadA and inhibits its activity.&lt;h4>Results&lt;/h4>In this study, based on the structural analysis, a chimeric CadA enzyme, CL2, was engineered by replacing its pH-sensitive region with a str</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 May</publication><modification>2026-06-01T22:21:51.171Z</modification><creation>2026-05-22T03:08:06.361Z</creation></dates><accession>S-EPMC12096693</accession><cross_references><pubmed>40405206</pubmed><doi>10.1186/s12934-025-02739-4</doi></cross_references></HashMap>