Cargando…

Regioselective para‐Carboxylation of Catechols with a Prenylated Flavin Dependent Decarboxylase

The utilization of CO(2) as a carbon source for organic synthesis meets the urgent demand for more sustainability in the production of chemicals. Herein, we report on the enzyme‐catalyzed para‐carboxylation of catechols, employing 3,4‐dihydroxybenzoic acid decarboxylases (AroY) that belong to the Ub...

Descripción completa

Detalles Bibliográficos
Autores principales:	Payer, Stefan E., Marshall, Stephen A., Bärland, Natalie, Sheng, Xiang, Reiter, Tamara, Dordic, Andela, Steinkellner, Georg, Wuensch, Christiane, Kaltwasser, Susann, Fisher, Karl, Rigby, Stephen E. J., Macheroux, Peter, Vonck, Janet, Gruber, Karl, Faber, Kurt, Himo, Fahmi, Leys, David, Pavkov‐Keller, Tea, Glueck, Silvia M.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	John Wiley and Sons Inc. 2017
Materias:	Communications
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5656893/ https://www.ncbi.nlm.nih.gov/pubmed/28857436 http://dx.doi.org/10.1002/anie.201708091

Ejemplares similares

Structural and biochemical characterization of the prenylated flavin mononucleotide-dependent indole-3-carboxylic acid decarboxylase
por: Gahloth, Deepankar, et al.
Publicado: (2022)

The role of conserved residues in Fdc decarboxylase in prenylated flavin mononucleotide oxidative maturation, cofactor isomerization, and catalysis
por: Bailey, Samuel S., et al.
Publicado: (2018)

Regioselective Enzymatic β‐Carboxylation of para‐Hydroxy‐ styrene Derivatives Catalyzed by Phenolic Acid Decarboxylases
por: Wuensch, Christiane, et al.
Publicado: (2015)

Exploring the Catalytic Promiscuity of Phenolic Acid Decarboxylases: Asymmetric, 1,6‐Conjugate Addition of Nucleophiles Across 4‐Hydroxystyrene
por: Payer, Stefan E., et al.
Publicado: (2017)

Regioselective Biocatalytic C4‐Prenylation of Unprotected Tryptophan Derivatives
por: Eggbauer, Bettina, et al.
Publicado: (2022)

Metal Ion Promiscuity and Structure of 2,3‐Dihydroxybenzoic Acid Decarboxylase of Aspergillus oryzae
por: Hofer, Gerhard, et al.
Publicado: (2020)

Effects of Active‐Site Modification and Quaternary Structure on the Regioselectivity of Catechol‐O‐Methyltransferase
por: Law, Brian J. C., et al.
Publicado: (2016)

Reaction Mechanism and Substrate Specificity of Iso-orotate Decarboxylase: A Combined Theoretical and Experimental Study
por: Sheng, Xiang, et al.
Publicado: (2018)

Regioselective Enzymatic Carboxylation of Phenols and Hydroxystyrene Derivatives
por: Wuensch, Christiane, et al.
Publicado: (2012)

The UbiX flavin prenyltransferase reaction mechanism resembles class I terpene cyclase chemistry
por: Marshall, Stephen A., et al.
Publicado: (2019)

Oxidation of Monolignols by Members of the Berberine Bridge Enzyme Family Suggests a Role in Plant Cell Wall Metabolism
por: Daniel, Bastian, et al.
Publicado: (2015)

UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis
por: White, Mark D., et al.
Publicado: (2015)

Genomic Determinants Encode the Reactivity and Regioselectivity of Flavin-Dependent Halogenases in Bacterial Genomes and Metagenomes
por: Jeon, Jehyun, et al.
Publicado: (2021)

A Rational Active-Site Redesign Converts a Decarboxylase into a C=C Hydratase: “Tethered Acetate” Supports Enantioselective Hydration of 4-Hydroxystyrenes
por: Payer, Stefan E., et al.
Publicado: (2018)

Inverting the Regioselectivity of the Berberine Bridge Enzyme by Employing Customized Fluorine-Containing Substrates
por: Resch, Verena, et al.
Publicado: (2012)

Structural basis of regioselective tryptophan dibromination by the single-component flavin-dependent halogenase AetF
por: Gäfe, Simon, et al.
Publicado: (2023)

Terminal Alkenes from Acrylic Acid Derivatives via Non‐Oxidative Enzymatic Decarboxylation by Ferulic Acid Decarboxylases
por: Aleku, Godwin A., et al.
Publicado: (2018)

Mechanisms of metal-dependent non-redox decarboxylases from quantum chemical calculations
por: Sheng, Xiang, et al.
Publicado: (2021)

A Theoretical Study of the Benzoylformate Decarboxylase Reaction Mechanism
por: Planas, Ferran, et al.
Publicado: (2018)

Structure and biochemical properties of recombinant human dimethylglycine dehydrogenase and comparison to the disease‐related H109R variant
por: Augustin, Peter, et al.
Publicado: (2016)

Enzymatic control of cycloadduct conformation ensures reversible 1,3 dipolar cycloaddition in a prFMN dependent decarboxylase
por: Bailey, Samuel S., et al.
Publicado: (2019)

Regioselective Enzymatic Carboxylation of Bioactive (Poly)phenols
por: Plasch, Katharina, et al.
Publicado: (2017)

Biocatalytic Enantioselective Oxidation of Sec‐Allylic Alcohols with Flavin‐Dependent Oxidases
por: Gandomkar, Somayyeh, et al.
Publicado: (2019)

Mechanism of 3‐Methylglutaconyl CoA Decarboxylase AibA/AibB: Pericyclic Reaction versus Direct Decarboxylation
por: Sheng, Xiang, et al.
Publicado: (2020)

Structure and Mechanism of Pseudomonas aeruginosa PA0254/HudA, a prFMN-Dependent Pyrrole-2-carboxylic Acid Decarboxylase Linked to Virulence
por: Payne, Karl A. P., et al.
Publicado: (2021)

Identification of promiscuous ene-reductase activity by mining structural databases using active site constellations
por: Steinkellner, Georg, et al.
Publicado: (2014)

Reduced Flavin: NMR investigation of N(5)-H exchange mechanism, estimation of ionisation constants and assessment of properties as biological catalyst
por: Macheroux, Peter, et al.
Publicado: (2005)

Broadening the Scope of the Flavin‐Tag Method by Improving Flavin Incorporation and Incorporating Flavin Analogs
por: Tong, Yapei, et al.
Publicado: (2022)

Activity-Based Probes for Studying the Activity of Flavin-Dependent Oxidases and for the Protein Target Profiling of Monoamine Oxidase Inhibitors**
por: Krysiak, Joanna M, et al.
Publicado: (2012)

Crystallization of domains involved in self-assembly of the S-layer protein SbsC
por: Đordić, Anđela, et al.
Publicado: (2012)

Substrate complexes of human dipeptidyl peptidase III reveal the mechanism of enzyme inhibition
por: Kumar, Prashant, et al.
Publicado: (2016)

Identification of Key Residues for Enzymatic Carboxylate Reduction
por: Stolterfoht, Holly, et al.
Publicado: (2018)

Extending the biocatalytic scope of regiocomplementary flavin-dependent halogenase enzymes
por: Shepherd, Sarah A., et al.
Publicado: (2015)

Directed evolution of prenylated FMN-dependent Fdc supports efficient in vivo isobutene production
por: Saaret, Annica, et al.
Publicado: (2021)

A basidomycetous hydroxynaphthalene-prenylating enzyme exhibits promiscuity toward prenyl donors
por: Martin, Andreas, et al.
Publicado: (2023)

A Self‐Assembling Flavin for Visible Photooxidation
por: Cariello, Michele, et al.
Publicado: (2022)

Flavine in Ophthalmic Practice
por: Ganguli, P.
Publicado: (1920)

Flavine in Ophthalmic Practice
por: Ganguli, P.
Publicado: (1921)

Flavine: the Ideal Antiseptic
Publicado: (1917)

The Antiseptic “Flavine” (Acriflavine)
Publicado: (1918)

Cannot write session to /tmp/vufind_sessions/sess_7hspr0ljfvj679amn2mc1mo5i8