Enzymes in “Green” Synthetic Chemistry: Laccase and Lipase

Molecules, Journal Year: 2024, Volume and Issue: 29(5), P. 989 - 989

Published: Feb. 24, 2024

Enzymes play an important role in numerous natural processes and are increasingly being utilized as environmentally friendly substitutes alternatives to many common catalysts. Their essential advantages high catalytic efficiency, substrate specificity, minimal formation of byproducts, low energy demand. All these benefits make enzymes highly desirable targets academic research industrial development. This review has the modest aim briefly overviewing classification, mechanism action, basic kinetics reaction condition effects that across all six enzyme classes. Special attention is devoted immobilization strategies main tools improve resistance environmental stress factors (temperature, pH solvents) prolong lifecycle biocatalysts. The drawbacks methods such macromolecular crosslinking, solid scaffold carriers, entrapment, surface modification (covalent physical) discussed illustrated using examples. Among hundreds possibly thousands known recently discovered enzymes, hydrolases oxidoreductases distinguished by their relative availability, stability, wide use synthetic applications, which include pharmaceutics, food beverage treatments, clean-up, polymerizations. Two representatives those groups-laccase (an oxidoreductase) lipase (a hydrolase)-are at length, including structure, mechanism, diverse usage. Objective representation current status emerging trends provided conclusions.

Language: Английский

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Advances, opportunities, and challenges in methods for interrogating the structure activity relationships of natural products

Natural Product Reports, Journal Year: 2024, Volume and Issue: 41(10), P. 1543 - 1578

Published: Jan. 1, 2024

This review highlights methods for studying structure activity relationships of natural products and proposes that these are complementary could be used to build an iterative computational-experimental workflow.

Language: Английский

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Catalytic performances of engineered and artificial heme peroxygenases

CHINESE JOURNAL OF CATALYSIS (CHINESE VERSION), Journal Year: 2025, Volume and Issue: 69, P. 35 - 51

Published: Feb. 1, 2025

Language: Английский

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C–C Bond Cleavage in the Late-Stage Biosynthesis of Huperzine Alkaloids Occurs via Enzymatic Retro-Aza-Prins Reaction

Journal of the American Chemical Society, Journal Year: 2025, Volume and Issue: unknown

Published: May 9, 2025

The demand for novel enzyme-catalyzed reactions in chemical synthesis has spurred the development of many new-to-nature reactions. Additionally, detailed analysis biosynthetic pathways can uncover unprecedented chemical/enzymatic mechanisms. In this study, we revisited catalytic mechanism 2-oxoglutarate-dependent dioxygenase Pt2OGD-1, involved biosynthesis huperzine alkaloids. Our experimental and computational investigations uncovered a previously unknown enzymatic C-C bond cleavage piperidine ring alkaloid scaffold, resembling an oxidative retro-aza-Prins reaction. Here, transformation is initiated by hydrogen abstraction, followed electron transfer at 4-position heterocycle, triggering opening finally resulting loss carbon atom as formaldehyde. This discovery expands toolbox reactions, enhances our understanding these enzymes, may facilitate their application biotechnological production pharmaceutically relevant scaffolds well biocatalysts with similar activities.

Language: Английский

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Highly Stereoselective Biocatalytic One-Pot Synthesis of Chiral Saturated Oxygen Heterocycles by Integration of a Biosynthetic Heterocyclase into Multiple-Enzyme Cascades

ACS Catalysis, Journal Year: 2024, Volume and Issue: 14(17), P. 13420 - 13428

Published: Aug. 23, 2024

The secondary metabolism is a rich source of enzymes with new synthetically attractive activities that have not yet been integrated into the toolbox biocatalysis. Chiral saturated oxygen heterocycles (CSOHs) are abundant structural elements natural products and other value-added compounds. We present biocatalytic method for synthesis CSOHs from readily accessible precursors combines an intramolecular oxa-Michael addition (IMOMA)-catalyzing cyclase (CYC) biosynthetic pathway alcohol dehydrogenases (ADHs) thioester-derivatizing enzymes. one-pot ADH–CYC reaction enables access to various tetrahydropyran (THP) tetrahydrofuran thioesters under control up four stereocenters. These convertible useful CSOH ketone, amide, aldehyde/alcohol, ester, carboxylic acid building blocks by chemical enzymatic means. extendibility more complex multienzyme cascades was demonstrated thioesterase reductase, allowing straightforward chemoenzymatic product (−)-civet, derivative, THP alcohol. integration IMOMA cyclases allows better exploitation high synthetic potential this group ring-forming expands repertoire pharmacologically relevant as highly selective versatile alternative. This approach will be adaptable wide range varying ADHs, cyclases, modifying

Language: Английский

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Discovery and Engineering of a Bacterial (+)‐Pulegone Reductase for Efficient (−)‐Menthol Biosynthesis

ChemSusChem, Journal Year: 2024, Volume and Issue: unknown

Published: June 11, 2024

The biosynthesis of valuable plant-derived monoterpene (-)-menthol from readily available feedstocks (e. g., (-)-limonene) is great significance because the high market demand for this product. However, biotransforming (+)-pulegone into (-)-menthone, precursor, through reductase (PGR) catalysis inefficient poor protein expression or catalytic efficiency (k

Language: Английский

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