AI Article Synopsis
- Baeyer-Villiger monooxygenases (BVMOs) have gained attention in recent years due to significant advancements in understanding their structure and mechanism, despite being discovered over 30 years ago.
- Major breakthroughs, such as determining BVMO crystal structures and discovering new variants, have sparked increased research and exploration of their biocatalytic potentials.
- The review discusses the current knowledge about BVMOs and highlights potential future industrial applications of these unique oxidative enzymes.
Article Abstract
Baeyer-Villiger monooxygenases For many enzyme classes, a wealth of information on, for example, structure and mechanism has been generated in the last few decades. While the first Baeyer-Villiger monooxygenases (BVMOs) were already isolated more than 30 years ago, detailed data on these enzymes were lacking until recently. Over the last years several major scientific breakthroughs, including the elucidation of BVMO crystal structures and the identification of numerous novel BVMOs, have boosted the research on BVMOs. This has led to intensified biocatalytic explorations of novel BVMOs and structure-inspired enzyme redesign. This review provides an overview on the recently gained knowledge on BVMOs and sketches the outlook for future industrial applications of these unique oxidative biocatalysts.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.cbpa.2009.11.017 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Engineering of a (R)-selective Baeyer-Villiger monooxygenase to minimize overoxidation activity for asymmetric synthesis of active pharmaceutical prazoles.
Int J Biol Macromol
January 2025
College of Bioscience and Bioengineering, Fuzhou University, Fuzhou 360105, China. Electronic address:
Baeyer-Villiger monooxygenases (BVMOs) can catalyze the asymmetric sulfoxidation to form pharmaceutical prazoles in environmentally friendly approach. In this work, the thermostable BVMO named PockeMO had high sulfoxidation activity towards rabeprazole sulfide to form (R)-rabeprazole but demonstrated significant overoxidation activity to form undesired sulfone by-product. To address this issue, the enzyme was engineered based on the computer assisted comparison for the substrate binding conformations.
View Article and Find Full Text PDFPyrrolizwilline, a Unique Bacterial Alkaloid Assembled by a Nonribosomal Peptide Synthetase and non-Enzymatic Dimerization.
Angew Chem Int Ed Engl
December 2024
Max Planck Institute for Terrestrial Microbiology, Department of Natural Products in Organismic Interactions, 35043, Marburg, Germany.
Article Synopsis
- Pyrrolizidine alkaloids (PAs) are a diverse group of compounds found in plants and bacteria, characterized by a specific chemical structure and produced through two main pathways (one in plants and another in bacteria).
- The study identified a gene cluster in the bacterium Xenorhabdus hominickii responsible for the production of a specific PA called pyrrolizwilline, shedding light on its biosynthesis.
- Researchers also characterized an important enzyme in the pathway, XhpG, utilizing advanced techniques like X-ray crystallography to understand its role in converting a precursor compound into pyrrolizwilline.
Characterization of the Baeyer-Villiger monooxygenase in the pathway of the bacterial pyrrolizidine alkaloids, legonmycins.
RSC Chem Biol
September 2024
Department of Chemistry, School of Natural and Computing Sciences, University of Aberdeen Aberdeen AB24 3UE UK
The Baeyer-Villiger monooxygenase (BVMO), LgnC, plays a crucial role in the biosynthesis of bacterial pyrrolizidine alkaloids, legonmycins. It processes bicyclic indolizidine substrates generated from the coordinative action of two non-ribosomal peptide synthetases (LgnB and LgnD) and the standalone type II thioesterase-like enzyme (LgnA). It has been demonstrated that the enzyme selectively inserts molecular oxygen into the carbon-carbon bond adjacent to the carbonyl group in legonindolizidines to form bicyclic 1,3-oxazepine carbamate intermediates.
View Article and Find Full Text PDFEmergence of a distinct mechanism of C-N bond formation in photoenzymes.
Nature
January 2025
Department of Chemistry, Princeton University, Princeton, NJ, USA.
Article Synopsis
- C-N bond formation is vital for creating nitrogen-containing compounds in pharmaceuticals and agricultural chemicals, with alkene hydroamination being a key method, but it has challenges in achieving stereoselectivity for complex structures.
- The researchers developed a novel photoenzymatic process using a mutated Baeyer-Villiger mono-oxygenase to efficiently produce 2,2-disubstituted pyrrolidines with high yield and stereoselectivity.
- This study highlights an innovative mechanism for C-N bond formation that leverages the enzyme’s environment, combining molecular dynamics simulations and protein engineering to tackle complex synthesis challenges in a way that traditional chemical methods cannot.
Discovery of a polyketide carboxylate phytotoxin from a polyketide glycoside hybrid by β-glucosidase mediated ester bond hydrolysis.
Chem Sci
September 2024
College of Pharmaceutical Sciences, Southwest University Chongqing 400715 P. R. China
Fungal phytotoxins cause significant harm to agricultural production or lead to plant diseases. Discovering new phytotoxins, dissecting their formation mechanism and understanding their action mode are important for controlling the harmful effects of fungal phytopathogens. In this study, a long-term unsolved cluster (polyketide synthase 16, PKS16 cluster) from species was thoroughly investigated and a series of new metabolites including both complex α-pyrone-polyketide glycosides and simple polyketide carboxylates were identified from .
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!