First and second sphere interactions accelerate non-native <i>N</i>-alkylation catalysis by the thermostable, methanol-tolerant B<sub>12</sub>-dependent enzyme MtaC-Reference-Cited by-同舟云学术

First and second sphere interactions accelerate non-native N-alkylation catalysis by the thermostable, methanol-tolerant B₁₂-dependent enzyme MtaC

Published:2023 Issue:32 Volume:59 Page:4798-4801
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Kumar Amardeep¹,Yang Xinhang¹,Li Jianbin¹,Lewis Jared C.¹^ORCID

Affiliation:

1. Department of Chemistry, Indiana University, Bloomington, IN, 47405, USA

Abstract

The corrinoid protein MtaC, which is natively involved in methyl transferase catalysis, catalyzes N-alkylation of aniline using ethyl diazoacetate.

Funder

Army Research Office

National Institutes of Health

National Science Foundation

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CC/D3CC01071F

Reference34 articles.

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