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A Hydroxyquinoline-Based Unnatural Amino Acid for the Design of Novel Artificial Metalloenzymes.

ABSTRACT: We have examined the potential of the noncanonical amino acid (8-hydroxyquinolin-3-yl)alanine (HQAla) for the design of artificial metalloenzymes. HQAla, a versatile chelator of late transition metals, was introduced into the lactococcal multidrug-resistance regulator (LmrR) by stop codon suppression methodology. LmrR_HQAla was shown to complex efficiently with three different metal ions, Cu^II , Zn^II and Rh^III to form unique artificial metalloenzymes. The catalytic potential of the Cu^II -bound LmrR_HQAla enzyme was shown through its ability to catalyse asymmetric Friedel-Craft alkylation and water addition, whereas the Zn^II -coupled enzyme was shown to mimic natural Zn hydrolase activity.

SUBMITTER: Drienovska I

PROVIDER: S-EPMC7689906 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature

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A Hydroxyquinoline-Based Unnatural Amino Acid for the Design of Novel Artificial Metalloenzymes.

Drienovská Ivana I Scheele Remkes A RA Gutiérrez de Souza Cora C Roelfes Gerard G

Chembiochem : a European journal of chemical biology 20200717 21

We have examined the potential of the noncanonical amino acid (8-hydroxyquinolin-3-yl)alanine (HQAla) for the design of artificial metalloenzymes. HQAla, a versatile chelator of late transition metals, was introduced into the lactococcal multidrug-resistance regulator (LmrR) by stop codon suppression methodology. LmrR_HQAla was shown to complex efficiently with three different metal ions, CuII , ZnII and RhIII to form unique artificial metalloenzymes. The catalyt ...[more]

PMID: 32585070

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