Issue 32, 2023

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

Abstract

The corrinoid protein MtaC, which is natively involved in methyl transferase catalysis, catalyzes N-alkylation of aniline using ethyl diazoacetate. Our results show how the native preference of B12 scaffolds for radical versus polar chemistry translates to non-native catalysis, which could guide selection of B12-dependent proteins for biocatalysis. MtaC also has high thermal stability and organic solvent tolerance, remaining folded even in pure methanol.

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

Supplementary files

Article information

Article type
Communication
Submitted
08 Mär 2023
Accepted
23 Mär 2023
First published
23 Mär 2023

Chem. Commun., 2023,59, 4798-4801

Author version available

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

A. Kumar, X. Yang, J. Li and J. C. Lewis, Chem. Commun., 2023, 59, 4798 DOI: 10.1039/D3CC01071F

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