Optimized Substrate Positioning Enables Switches in the C–H Cleavage Site and Reaction Outcome in the Hydroxylation–Epoxidation Sequence Catalyzed by Hyoscyamine 6β-Hydroxylase-Reference-Cited by-同舟云学术

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Optimized Substrate Positioning Enables Switches in the C–H Cleavage Site and Reaction Outcome in the Hydroxylation–Epoxidation Sequence Catalyzed by Hyoscyamine 6β-Hydroxylase

Published:2024-08-22 Issue:35 Volume:146 Page:24271-24287
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Wenger Eliott S.¹^ORCID,Martinie Ryan J.^ORCID,Ushimaru Richiro²^ORCID,Pollock Christopher J.^ORCID,Sil Debangsu^ORCID,Li Aaron,Hoang Nhi,Palowitch Gavin M.,Graham Brandt P.,Schaperdoth Irene^ORCID,Burke Evan J.^ORCID,Maggiolo Ailiena O.,Chang Wei-chen^ORCID,Allen Benjamin D.,Krebs Carsten^ORCID,Silakov Alexey,Boal Amie K.^ORCID,Bollinger J. Martin^ORCID

Affiliation:

1. Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States

2. Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-8657, Japan

Funder

National Institute of General Medical Sciences

National Science Foundation

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.4c04406

Reference68 articles.

1. Nature’s Machinery, Repurposed: Expanding the Repertoire of Iron-Dependent Oxygenases

2. Engineering Hydroxylase Activity, Selectivity, and Stability for a Scalable Concise Synthesis of a Key Intermediate to Belzutifan

3. Rational Design of the Spatial Effect in a Fe(II)/α‐Ketoglutarate‐Dependent Dioxygenase Reverses the Regioselectivity of C(sp³)−H Bond Hydroxylation in Aliphatic Amino Acids

4. Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes

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