کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
6451429 | 1416324 | 2017 | 10 صفحه PDF | دانلود رایگان |
- Engineered hemoproteins expand the biocatalytic repertoire.
- Different hemoprotein scaffolds offer diverse activities and selectivities.
- New enzymes enable preparative-scale syntheses of pharmaceutical intermediates.
- Insights into factors limiting enzyme lifetime offer new options for engineering.
The surge in reports of heme-dependent proteins as catalysts for abiotic, synthetically valuable carbene and nitrene transfer reactions dramatically illustrates the evolvability of the protein world and our nascent ability to exploit that for new enzyme chemistry. We highlight the latest additions to the hemoprotein-catalyzed reaction repertoire (including carbene Si-H and C-H insertions, Doyle-Kirmse reactions, aldehyde olefinations, azide-to-aldehyde conversions, and intermolecular nitrene C-H insertion) and show how different hemoprotein scaffolds offer varied reactivity and selectivity. Preparative-scale syntheses of pharmaceutically relevant compounds accomplished with these new catalysts are beginning to demonstrate their biotechnological relevance. Insights into the determinants of enzyme lifetime and product yield are providing generalizable cues for engineering heme-dependent proteins to further broaden the scope and utility of these non-natural activities.
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Journal: Current Opinion in Biotechnology - Volume 47, October 2017, Pages 102-111