<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Li N</submitter><funding>Fundamental Research Funds for the Central Universities</funding><funding>National First-class Discipline Program of Light Industry Technology and Engineering</funding><funding>National Natural Science Foundation of China</funding><funding>Jiangsu Postdoctoral Research Funding Program</funding><funding>National Key Research and Development Program of China</funding><pagination>27</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8922893</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>15(1)</volume><pubmed_abstract>&lt;h4>Background&lt;/h4>O-Acetyl-L-homoserine (OAH) is an important potential platform chemical. However, low levels of production of OAH are greatly limiting its industrial application. Furthermore, as a common and safe amino acid-producing strain, Corynebacterium glutamicum has not yet achieved efficient production of OAH.&lt;h4>Results&lt;/h4>First, exogenous L-homoserine acetyltransferase was introduced into an L-homoserine-producing strain, resulting in the accumulation of 0.98 g/L of OAH. Second, by comparing different acetyl-CoA biosynthesis pathways and adding several feedstocks (acetate, citrate, and pantothenate), the OAH titer increased 2.3-fold to 3.2 g/L. Then, the OAH titer further increased by 62.5% when the expression of L-homoserine dehydrogenase and L-homoserine acetyltransferase was strengthened via strong promoters. Finally, the engineered strain produced 17.4 g/L of OAH in 96 h with acetate as the supplementary feedstock in a 5-L bioreactor.&lt;h4>Conclusions&lt;/h4>This is the first report on the efficient production of OAH with C. glutamicum as the chassis, which would provide a good foundation for industrial production of OAH.</pubmed_abstract><journal>Biotechnology for biofuels and bioproducts</journal><pubmed_title>O-Acetyl-L-homoserine production enhanced by pathway strengthening and acetate supplementation in Corynebacterium glutamicum.</pubmed_title><pmcid>PMC8922893</pmcid><funding_grant_id>2021K171B</funding_grant_id><funding_grant_id>22108098</funding_grant_id><funding_grant_id>JUSRP121118</funding_grant_id><funding_grant_id>LITE2018-08</funding_grant_id><funding_grant_id>2019YFA0904800</funding_grant_id><pubmed_authors>Xu S</pubmed_authors><pubmed_authors>Zeng W</pubmed_authors><pubmed_authors>Li N</pubmed_authors><pubmed_authors>Zhou J</pubmed_authors></additional><is_claimable>false</is_claimable><name>O-Acetyl-L-homoserine production enhanced by pathway strengthening and acetate supplementation in Corynebacterium glutamicum.</name><description>&lt;h4>Background&lt;/h4>O-Acetyl-L-homoserine (OAH) is an important potential platform chemical. However, low levels of production of OAH are greatly limiting its industrial application. Furthermore, as a common and safe amino acid-producing strain, Corynebacterium glutamicum has not yet achieved efficient production of OAH.&lt;h4>Results&lt;/h4>First, exogenous L-homoserine acetyltransferase was introduced into an L-homoserine-producing strain, resulting in the accumulation of 0.98 g/L of OAH. Second, by comparing different acetyl-CoA biosynthesis pathways and adding several feedstocks (acetate, citrate, and pantothenate), the OAH titer increased 2.3-fold to 3.2 g/L. Then, the OAH titer further increased by 62.5% when the expression of L-homoserine dehydrogenase and L-homoserine acetyltransferase was strengthened via strong promoters. Finally, the engineered strain produced 17.4 g/L of OAH in 96 h with acetate as the supplementary feedstock in a 5-L bioreactor.&lt;h4>Conclusions&lt;/h4>This is the first report on the efficient production of OAH with C. glutamicum as the chassis, which would provide a good foundation for industrial production of OAH.</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Mar</publication><modification>2025-04-26T19:11:05.185Z</modification><creation>2025-04-06T16:00:37.669Z</creation></dates><accession>S-EPMC8922893</accession><cross_references><pubmed>35287716</pubmed><doi>10.1186/s13068-022-02114-0</doi></cross_references></HashMap>