ArticleChembiochem : a European journal of chemical biology2021
Discovery, Biocatalytic Exploration and Structural Analysis of a 4-Ethylphenol Oxidase from Gulosibacter chungangensis.
Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- Discovery of a new subfamily expands the catalytic versatility of vanillyl alcohol oxidases.Frontiers in microbiology · 2026Article
- A Rare Case ofInfection and drug resistance · 2026Article
- Bioinformatics and Computationally Supported Redesign of Aspartase for β-Alanine Synthesis by Acrylic Acid Hydroamination.ACS catalysis · 2025Article
- Emergency wound site infection caused by Gulosibacter massiliensis: a case report.BMC infectious diseases · 2024Article
- Substrate scope expansion of 4-phenol oxidases by rational enzyme selection and sequence-function relations.Communications chemistry · 2024Article
- Vanillyl alcohol oxidase from Diplodia corticola: Residues Ala420 and Glu466 allow for efficient catalysis of syringyl derivatives.The Journal of biological chemistry · 2023Article
- Structure- and computational-aided engineering of an oxidase to produce isoeugenol from a lignin-derived compound.Nature communications · 2022Article
- Discovery, Biocatalytic Exploration and Structural Analysis of a 4-Ethylphenol Oxidase from Gulosibacter chungangensis.Chembiochem : a European journal of chemical biology · 2021Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The vanillyl-alcohol oxidase (VAO) family is a rich source of biocatalysts for the oxidative bioconversion of phenolic compounds. Through genome mining and sequence comparisons, we found that several family members lack a generally conserved catalytic aspartate. This finding led us to study a VAO-homolog featuring a glutamate residue in place of the common aspartate. This 4-ethylphenol oxidase from Gulosibacter chungangensis (Gc4EO) shares 42 % sequence identity with VAO from Penicillium simplicissimum, contains the same 8α-N
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Registered trials
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