ArticleBiochemistry2018
Mechanism and Structure of γ-Resorcylate Decarboxylase.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 38 citations in OpenAlex.
- The Factors Governing Metal Dependence of an Emergent Superfamily of Bimetallic Oxygenases.Journal of the American Chemical Society · 2026Article
- Bioinformatic Discovery of a Cambialistic Monooxygenase.Journal of the American Chemical Society · 2024Article
- De novo biosynthesis of 2-hydroxyterephthalic acid, the monomer for high-performance hydroxyl modified PBO fiber, by enzymatic Kolbe-Schmitt reaction with COBiotechnology for biofuels and bioproducts · 2023Article
- Characterization of the depsidone gene cluster reveals etherification, decarboxylation and multiple halogenations as tailoring steps in depsidone assembly.Acta pharmaceutica Sinica. B · 2023Article
- Enzymatic Conversion of COChemical reviews · 2023Review
- The Quantum Chemical Cluster Approach in Biocatalysis.Accounts of chemical research · 2023Review
- Metal Ion Promiscuity and Structure of 2,3-Dihydroxybenzoic Acid Decarboxylase of Aspergillus oryzae.Chembiochem : a European journal of chemical biology · 2021Article
- Crystal structures of non-oxidative decarboxylases reveal a new mechanism of action with a catalytic dyad and structural twists.Scientific reports · 2021Article
- Mechanisms of metal-dependent non-redox decarboxylases from quantum chemical calculations.Computational and structural biotechnology journal · 2021Review
- Non-Oxidative Enzymatic (De)Carboxylation of (Hetero)Aromatics and Acrylic Acid Derivatives.Advanced synthesis & catalysis · 2019Review
- Reaction Mechanism and Substrate Specificity ofFrontiers in chemistry · 2018Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
γ-Resorcylate decarboxylase (γ-RSD) has evolved to catalyze the reversible decarboxylation of 2,6-dihydroxybenzoate to resorcinol in a nonoxidative fashion. This enzyme is of significant interest because of its potential for the production of γ-resorcylate and other benzoic acid derivatives under environmentally sustainable conditions. Kinetic constants for the decarboxylation of 2,6-dihydroxybenzoate catalyzed by γ-RSD from Polaromonas sp. JS666 are reported, and the enzyme is shown to be active with 2,3-dihydroxybenzoate, 2,4,6-trihydroxybenzoate, and 2,6-dihydroxy-4-methylbenzoate. The three-dimensional structure of γ-RSD with the inhibitor 2-nitroresorcinol (2-NR) bound in the active site is reported. 2-NR is directly ligated to a Mn
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.