{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shang HQ"],"funding":["National Natural Science Foundation of China"],"pagination":["e70018"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11968058"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["25(4)"],"pubmed_abstract":["Ferulic acid is a high-value chemical synthesized in plants. The ferulic acid biosynthesis is still affected by the insufficient methylation activity of caffeic acid O-methyltransferase (<i>COMT</i>). In this study, we engineered <i>COMT</i> from <i>Arabidopsis thaliana</i> to match caffeic acid, and the mutant <i>COMT</i> <sup>N129V-H313A-F174L</sup> showed 4.19-fold enhanced catalytic efficiency for degrading caffeic acid. Then, we constructed the de novo synthesis pathway of ferulic acid by introducing tyrosine ammonia lyase from <i>Flavobacterium johnsoniae</i> (<i>FjTAL</i>), 4-hydroxyphenylacetate 3-hydroxylase from <i>Escherichia coli</i> (<i>EcHpaBC</i>), and mutant <i>COMT</i> <sup>N129V-H313A-F174L</sup>, and further increased tyrosine synthesis. Furthermore, we overexpressed two"],"journal":["Engineering in life sciences"],"pubmed_title":["Engineering Caffeic Acid O-Methyltransferase for Efficient De Novo Ferulic Acid Synthesis."],"pmcid":["PMC11968058"],"funding_grant_id":["32172145"],"pubmed_authors":["Chen QH","Qiang S","Hu CY","Zhang CQ","Meng YH","Shang HQ","Zheng R","Bo Yang Q"],"additional_accession":[]},"is_claimable":false,"name":"Engineering Caffeic Acid O-Methyltransferase for Efficient De Novo Ferulic Acid Synthesis.","description":"Ferulic acid is a high-value chemical synthesized in plants. The ferulic acid biosynthesis is still affected by the insufficient methylation activity of caffeic acid O-methyltransferase (<i>COMT</i>). In this study, we engineered <i>COMT</i> from <i>Arabidopsis thaliana</i> to match caffeic acid, and the mutant <i>COMT</i> <sup>N129V-H313A-F174L</sup> showed 4.19-fold enhanced catalytic efficiency for degrading caffeic acid. Then, we constructed the de novo synthesis pathway of ferulic acid by introducing tyrosine ammonia lyase from <i>Flavobacterium johnsoniae</i> (<i>FjTAL</i>), 4-hydroxyphenylacetate 3-hydroxylase from <i>Escherichia coli</i> (<i>EcHpaBC</i>), and mutant <i>COMT</i> <sup>N129V-H313A-F174L</sup>, and further increased tyrosine synthesis. Furthermore, we overexpressed two","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Apr","modification":"2026-06-03T04:45:18.618Z","creation":"2025-07-09T03:04:56.114Z"},"accession":"S-EPMC11968058","cross_references":{"pubmed":["40190727"],"doi":["10.1002/elsc.70018"]}}