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

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 B 12 scaffolds for radical versus polar chemistry translates to non-native catalysis, which could guide s...

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Published in:Chemical communications (Cambridge, England) England), 2023-04, Vol.59 (32), p.4798-481
Main Authors: Kumar, Amardeep, Yang, Xinhang, Li, Jianbin, Lewis, Jared C
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Summary: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 B 12 scaffolds for radical versus polar chemistry translates to non-native catalysis, which could guide selection of B 12 -dependent proteins for biocatalysis. MtaC also has high thermal stability and organic solvent tolerance, remaining folded even in pure methanol. The corrinoid protein MtaC, which is natively involved in methyl transferase catalysis, catalyzes N -alkylation of aniline using ethyl diazoacetate.
ISSN:1359-7345
1364-548X
DOI:10.1039/d3cc01071f