{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["14(1)"],"submitter":["Alpdagtas S"],"funding":["Scientific and Technological Research Council of Turkey","Heinrich-Heine-Universität Düsseldorf","Ministry of Innovation, Science and Research of the German State of North Rhine-Westphalia"],"pubmed_abstract":["Glyoxal oxidases, belonging to the group of copper radical oxidases (CROs), oxidize aldehydes to carboxylic acids, while reducing O<sub>2</sub> to H<sub>2</sub>O<sub>2</sub>. Their activity on furan derivatives like 5-hydroxymethylfurfural (HMF) makes these enzymes promising biocatalysts for the environmentally friendly synthesis of the bioplastics precursor 2,5-furandicarboxylic acid (FDCA). However, glyoxal oxidases suffer from inactivation, which requires the identification of suitable redox activators for efficient substrate conversion. Furthermore, only a few glyoxal oxidases have been expressed and characterized so far. Here, we report on a new glyoxal oxidase from Trametes versicolor (TvGLOX) that was expressed at high levels in Pichia pastoris (reclassified as Komagataella phaffii)"],"journal":["Scientific reports"],"pagination":["5932"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10928124"],"repository":["biostudies-literature"],"pubmed_title":["Identification of redox activators for continuous reactivation of glyoxal oxidase from Trametes versicolor in a two-enzyme reaction cascade."],"pmcid":["PMC10928124"],"pubmed_authors":["Urlacher VB","Jankowski N","Koschorreck K","Alpdagtas S"],"additional_accession":[]},"is_claimable":false,"name":"Identification of redox activators for continuous reactivation of glyoxal oxidase from Trametes versicolor in a two-enzyme reaction cascade.","description":"Glyoxal oxidases, belonging to the group of copper radical oxidases (CROs), oxidize aldehydes to carboxylic acids, while reducing O<sub>2</sub> to H<sub>2</sub>O<sub>2</sub>. Their activity on furan derivatives like 5-hydroxymethylfurfural (HMF) makes these enzymes promising biocatalysts for the environmentally friendly synthesis of the bioplastics precursor 2,5-furandicarboxylic acid (FDCA). However, glyoxal oxidases suffer from inactivation, which requires the identification of suitable redox activators for efficient substrate conversion. Furthermore, only a few glyoxal oxidases have been expressed and characterized so far. Here, we report on a new glyoxal oxidase from Trametes versicolor (TvGLOX) that was expressed at high levels in Pichia pastoris (reclassified as Komagataella phaffii)","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-07-15T04:35:17.749Z","creation":"2024-11-15T12:26:34.217Z"},"accession":"S-EPMC10928124","cross_references":{"pubmed":["38467766"],"doi":["10.1038/s41598-024-56429-z"]}}