{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yang K"],"funding":["Zhejiang Natural Science Foundation","National Natural Science Foundation of China"],"pagination":["6699"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10537072"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["28(18)"],"pubmed_abstract":["Catechols have important applications in the pharmaceutical, food, cosmetic, and functional material industries. 4-hydroxyphenylacetate-3-hydroxylase (4HPA3H), a two-component enzyme system comprising HpaB (monooxygenase) and HpaC (FAD oxidoreductase), demonstrates significant potential for catechol production because it can be easily expressed, is highly active, and exhibits <i>ortho</i>-hydroxylation activity toward a broad spectrum of phenol substrates. HpaB determines the <i>ortho</i>-hydroxylation efficiency and substrate spectrum of the enzyme; therefore, studying its structure-activity relationship, improving its properties, and developing a robust HpaB-conducting system are of significance and value; indeed, considerable efforts have been made in these areas in recent decades. Here"],"journal":["Molecules (Basel, Switzerland)"],"pubmed_title":["Advances in 4-Hydroxyphenylacetate-3-hydroxylase Monooxygenase."],"pmcid":["PMC10537072"],"funding_grant_id":["LY23B060001","32071268","32071268, 31971372","31971372","LY21B060003","32371542","LY21B060003, LY23B060001"],"pubmed_authors":["Mei L","Hu S","Yang K","Huang J","Mei J","Zhao W","Lv C","Zhang Q"],"additional_accession":[]},"is_claimable":false,"name":"Advances in 4-Hydroxyphenylacetate-3-hydroxylase Monooxygenase.","description":"Catechols have important applications in the pharmaceutical, food, cosmetic, and functional material industries. 4-hydroxyphenylacetate-3-hydroxylase (4HPA3H), a two-component enzyme system comprising HpaB (monooxygenase) and HpaC (FAD oxidoreductase), demonstrates significant potential for catechol production because it can be easily expressed, is highly active, and exhibits <i>ortho</i>-hydroxylation activity toward a broad spectrum of phenol substrates. HpaB determines the <i>ortho</i>-hydroxylation efficiency and substrate spectrum of the enzyme; therefore, studying its structure-activity relationship, improving its properties, and developing a robust HpaB-conducting system are of significance and value; indeed, considerable efforts have been made in these areas in recent decades. Here","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Sep","modification":"2026-04-08T14:31:43.641Z","creation":"2025-02-19T00:00:46.168Z"},"accession":"S-EPMC10537072","cross_references":{"pubmed":["37764475"],"doi":["10.3390/molecules28186699"]}}