ArticleJournal of the American Chemical Society2016
Substrate Distortion and the Catalytic Reaction Mechanism of 5-Carboxyvanillate Decarboxylase.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 49 citations in OpenAlex.
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- Metal Ion Promiscuity and Structure of 2,3-Dihydroxybenzoic Acid Decarboxylase of Aspergillus oryzae.Chembiochem : a European journal of chemical biology · 2021Article
- Mechanisms of metal-dependent non-redox decarboxylases from quantum chemical calculations.Computational and structural biotechnology journal · 2021Review
- Synthesis, crystal structure and spectroscopic and Hirshfeld surface analysis of 4-hy-droxy-3-meth-oxy-5-nitro-benzaldehyde.Acta crystallographica. Section E, Crystallographic communications · 2020Article
- Exploring the substrate scope of ferulic acid decarboxylase (FDC1) from Saccharomyces cerevisiae.Scientific reports · 2019Article
- Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition.Journal of visualized experiments : JoVE · 2018Article
- Mechanism and Structure of γ-Resorcylate Decarboxylase.Biochemistry · 2018Article
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- Reaction Mechanism and Substrate Specificity ofFrontiers in chemistry · 2018Article
- Article
- QM Cluster or QM/MM in Computational Enzymology: The Test Case of LigW-Decarboxylase.Frontiers in chemistry · 2018Article
- The bacterialThe Journal of biological chemistry · 2017Article
- Primary Deuterium Kinetic Isotope Effects From Product Yields: Rationale, Implementation, and Interpretation.Methods in enzymology · 2017Article
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
5-Carboxyvanillate decarboxylase (LigW) catalyzes the conversion of 5-carboxyvanillate to vanillate in the biochemical pathway for the degradation of lignin. This enzyme was shown to require Mn(2+) for catalytic activity and the kinetic constants for the decarboxylation of 5-carboxyvanillate by the enzymes from Sphingomonas paucimobilis SYK-6 (kcat = 2.2 s(-1) and kcat/Km = 4.0 × 10(4) M(-1) s(-1)) and Novosphingobium aromaticivorans (kcat = 27 s(-1) and kcat/Km = 1.1 × 10(5) M(-1) s(-1)) were determined. The three-dimensional structures of both enzymes were determined in the presence and absence of ligands bound in the active site. The structure of LigW from N. aromaticivorans, bound with the substrate analogue, 5-nitrovanillate (Kd = 5.0 nM), was determined to a resolution of 1.07 Å. The structure of this complex shows a remarkable enzyme-induced distortion of the nitro-substituent out of the plane of the phenyl ring by approximately 23°. A chemical reaction mechanism for the decarboxylation of 5-carboxyvanillate by LigW was proposed on the basis of the high resolution X-ray structures determined in the presence ligands bound in the active site, mutation of active site residues, and the magnitude of the product isotope effect determined in a mixture of H2O and D2O. In the proposed reaction mechanism the enzyme facilitates the transfer of a proton to C5 of the substrate prior to the decarboxylation step.
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