ReviewCurrent opinion in chemical biology2012
Current developments and challenges in the search for a naturally selected Diels-Alderase.
Review in Current opinion in chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
25 citing papers in PubMed.
- Interrogation of an Enzyme Library Reveals the Catalytic Plasticity of Naturally Evolved [4+2] Cyclases.Chembiochem : a European journal of chemical biology · 2023Article
- Recent advances on Pestalotiopsis genus: chemistry, biological activities, structure-activity relationship, and biosynthesis.Archives of pharmacal research · 2023Review
- Mechanism of the Stereoselective Catalysis of Diels-Alderase PyrE3 Involved in Pyrroindomycin Biosynthesis.Journal of the American Chemical Society · 2022Article
- Peculiarities of meroterpenoids and their bioproduction.Applied microbiology and biotechnology · 2021Review
- Catalytic mechanism andNature catalysis · 2021Article
- Biosynthesis of Grandione: An Example of Tandem Hetero Diels-Alder/Retro-Claisen Rearrangement Reaction?Molecules (Basel, Switzerland) · 2018Article
- Natural products as inspiration for the development of new synthetic methods.Journal of the Chinese Chemical Society. Zhongguo hua xue hui (Taipei, Taiwan) · 2018Article
- Computational Insights into an Enzyme-Catalyzed [4+2] Cycloaddition.The Journal of organic chemistry · 2017Article
- Structural insights into enzymatic [4+2]Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Natural [4 + 2]-Cyclases.Chemical reviews · 2017Review
- The Enzymology of Organic Transformations: A Survey of Name Reactions in Biological Systems.Angewandte Chemie (International ed. in English) · 2017Review
- Biochemical Characterization of a Eukaryotic Decalin-Forming Diels-Alderase.Journal of the American Chemical Society · 2016Article
- Genome mining of the sordarin biosynthetic gene cluster from Sordaria araneosa Cain ATCC 36386: characterization of cycloaraneosene synthase and GDP-6-deoxyaltrose transferase.The Journal of antibiotics · 2016Article
- Recent advances of Diels-Alderases involved in natural product biosynthesis.The Journal of antibiotics · 2016Review
- Dynamically Complex [6+4] and [4+2] Cycloadditions in the Biosynthesis of Spinosyn A.Journal of the American Chemical Society · 2016Article
- Natural Diels-Alderases: Elusive and Irresistable.The Journal of organic chemistry · 2015Article
- Quo vadis, enzymology?Nature chemical biology · 2015Article
- The structure of SpnF, a standalone enzyme that catalyzes [4 + 2] cycloaddition.Nature chemical biology · 2015Article
- An enzymatic [4+2] cyclization cascade creates the pentacyclic core of pyrroindomycins.Nature chemical biology · 2015Article
- Squalene hopene cyclases are protonases for stereoselective Brønsted acid catalysis.Nature chemical biology · 2015Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Only a very few examples of enzymes known to catalyze pericyclic reactions have been reported, and presently no enzyme has been demonstrated unequivocally to catalyze a Diels-Alder reaction. Nevertheless, research into secondary metabolism has led to the discovery of numerous natural products exhibiting the structural hallmarks of [4+2] cycloadditions, prompting efforts to characterize the responsible enzymatic processes. These efforts have resulted in a growing collection of enzymes believed to catalyze pericyclic [4+2] cycloaddition reactions; however, in each case the complexity of the substrates and catalytic properties of these enzymes poses significant challenges in substantiating these hypotheses. Herein we consider the principles motivating these efforts and the enzymological systems currently under investigation.
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Registered trials
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.