{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["11"],"submitter":["Liu X"],"pubmed_abstract":["L-threonine dehydrogenase (TDH) is a rate-limiting enzyme in the biosynthesis pathway of 2,5-dimethylpyrazine and 2,3,5-trimethylpyrazine, which are widely used food additives. However, natural TDH enzymes suffer from low catalytic activity and poor environmental adaptability, limiting their industrial applications. This study hypothesized that strategic site-directed mutagenesis of conserved amino acid residues within the substrate-binding pocket and catalytic domain could affect both enzymatic activity and environmental stability of TDH. To test this hypothesis, BlTDH from <i>Bacillus licheniformis</i> was selected as the target enzyme, and structure-oriented alanine substitution mutagenesis was systematically applied to five conserved residues (T94, H95, N157, T293, and G294). The resul"],"journal":["Food chemistry. Molecular sciences"],"pagination":["100272"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12276384"],"repository":["biostudies-literature"],"pubmed_title":["Improving enzymatic properties of BlTDH from &lt;i&gt;Bacillus licheniformis&lt;/i&gt; through site-directed mutagenesis."],"pmcid":["PMC12276384"],"pubmed_authors":["Liu X","Li H","Tang Z","Gu H","Chen S","Quan W"],"additional_accession":[]},"is_claimable":false,"name":"Improving enzymatic properties of BlTDH from &lt;i&gt;Bacillus licheniformis&lt;/i&gt; through site-directed mutagenesis.","description":"L-threonine dehydrogenase (TDH) is a rate-limiting enzyme in the biosynthesis pathway of 2,5-dimethylpyrazine and 2,3,5-trimethylpyrazine, which are widely used food additives. However, natural TDH enzymes suffer from low catalytic activity and poor environmental adaptability, limiting their industrial applications. This study hypothesized that strategic site-directed mutagenesis of conserved amino acid residues within the substrate-binding pocket and catalytic domain could affect both enzymatic activity and environmental stability of TDH. To test this hypothesis, BlTDH from <i>Bacillus licheniformis</i> was selected as the target enzyme, and structure-oriented alanine substitution mutagenesis was systematically applied to five conserved residues (T94, H95, N157, T293, and G294). The resul","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Dec","modification":"2026-03-27T16:18:25.67Z","creation":"2025-08-30T03:05:59.65Z"},"accession":"S-EPMC12276384","cross_references":{"pubmed":["40687379"],"doi":["10.1016/j.fochms.2025.100272"]}}