Erratum: Corrigendum: A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo

Coelho, Pedro Simões; Wang, Z Jane; Ener, Maraia E.; Baril, S.A.; Kannan, Arvind; Arnold, Frances H.; Brustad, Eric M.

doi:10.1038/nchembio0214-164d

Cited by 2 publications

(1 citation statement)

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“…57 Specialisation through mutation has been employed to tune product distributions obtained from promiscuous natural enzymes, 61 and to unlock new-to-nature reactivities in engineered enzymes. 62 Here we have shown that we can exploit this effect in promiscuous enzymes that operate with non-canonical catalytic machinery in order to specialise them towards selective and useful transformations (Figure 4).…”

Section: Substrate Scopementioning

confidence: 97%

Unlocking Iminium Catalysis in Artificial Enzymes to Create a Friedel-Crafts Alkylase

Leveson-Gower¹,

Zhou²,

Drienovská³

et al. 2021

Preprint

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We show that the incorporation of the non-canonical amino acid para-aminophenylalanine (pAF) into the non-enzymatic protein scaffold LmrR creates a proficient and stereoselective artificial enzyme (LmrR_pAF) for the vinylogous Friedel-crafts alkylation between alpha, beta-unsaturated aldehydes and indoles. pAF acts as a catalytic residue, activating enal substrates towards conjugate addition via the formation of intermediate iminium ion species, whilst the protein scaffold provides rate acceleration and enantio-induction. Improved LmrR_pAF varants were identified by direted evolution advised by alanine-scanning to obtain a triple mutant that provided higher yields and enantioselectivities for a range of enals and indoles. Analys of Michaelis-Menten kinetics of LmrR-pAF and tevolved mutants reveals that new activities emerge via evolutionary pathways that diverge from one another and specialise catalytic reactivity.<br>

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Section: Substrate Scopementioning

confidence: 97%