<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>3(2)</volume><submitter>Yao L</submitter><pubmed_abstract>Biosynthesis of the functional factor γ-aminobutyric acid (GABA) in bacteria involves two key proteins an intracellular glutamate decarboxylase (GadB) and a membrane-bound antiporter (GadC). Efficient co-expression of suitable GadB and GadC candidates is crucial for improving GABA productivity. In this study, &lt;i>gadB&lt;/i> &lt;sub>ΔC11&lt;/sub> of &lt;i>Lactiplantibacillus plantarum&lt;/i> and &lt;i>gadC&lt;/i> &lt;sub>ΔC41&lt;/sub> of &lt;i>Escherichia coli&lt;/i> were inserted into the designed double promoter (P &lt;i>&lt;sub>T7lac&lt;/sub>&lt;/i> and P &lt;i>&lt;sub>BAD&lt;/sub>&lt;/i> ) expression system. Then, &lt;i>E. coli&lt;/i> Lemo21(DE3) was chosen as the host to minimize the toxic effects of GadC&lt;sub>ΔC41&lt;/sub> overexpression. Furthermore, a green and high-efficiency GABA synthesis system using dormant engineered Lemo21(DE3) cells as bioc</pubmed_abstract><journal>Engineering microbiology</journal><pagination>100077</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11610993</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>High-level production of γ-aminobutyric acid via efficient co-expression of the key genes of glutamate decarboxylase system in &amp;lt;i&amp;gt;Escherichia coli&amp;lt;/i&amp;gt;.</pubmed_title><pmcid>PMC11610993</pmcid><pubmed_authors>Yao L</pubmed_authors><pubmed_authors>Mei L</pubmed_authors><pubmed_authors>Hu S</pubmed_authors><pubmed_authors>Cao H</pubmed_authors><pubmed_authors>Huang J</pubmed_authors><pubmed_authors>Zhao W</pubmed_authors><pubmed_authors>Lyu C</pubmed_authors><pubmed_authors>Wang Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>High-level production of γ-aminobutyric acid via efficient co-expression of the key genes of glutamate decarboxylase system in &amp;lt;i&amp;gt;Escherichia coli&amp;lt;/i&amp;gt;.</name><description>Biosynthesis of the functional factor γ-aminobutyric acid (GABA) in bacteria involves two key proteins an intracellular glutamate decarboxylase (GadB) and a membrane-bound antiporter (GadC). Efficient co-expression of suitable GadB and GadC candidates is crucial for improving GABA productivity. In this study, &lt;i>gadB&lt;/i> &lt;sub>ΔC11&lt;/sub> of &lt;i>Lactiplantibacillus plantarum&lt;/i> and &lt;i>gadC&lt;/i> &lt;sub>ΔC41&lt;/sub> of &lt;i>Escherichia coli&lt;/i> were inserted into the designed double promoter (P &lt;i>&lt;sub>T7lac&lt;/sub>&lt;/i> and P &lt;i>&lt;sub>BAD&lt;/sub>&lt;/i> ) expression system. Then, &lt;i>E. coli&lt;/i> Lemo21(DE3) was chosen as the host to minimize the toxic effects of GadC&lt;sub>ΔC41&lt;/sub> overexpression. Furthermore, a green and high-efficiency GABA synthesis system using dormant engineered Lemo21(DE3) cells as bioc</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Jun</publication><modification>2025-04-27T02:10:55.243Z</modification><creation>2025-04-06T18:31:29.107Z</creation></dates><accession>S-EPMC11610993</accession><cross_references><pubmed>39629248</pubmed><doi>10.1016/j.engmic.2023.100077</doi></cross_references></HashMap>