Published October 20, 2018 | Version Pre-print
Journal article Open

Cloning and characterization of a new delta-specific l-leucine dioxygenase from Anabaena variabilis

Authors/Creators

  • 1. Ruhr University Bochum
  • 2. Graz University of Technology

Description

Highlights

•A new, δ-specific cyanobacterial amino acid dioxygenase was isolated and recombinantly expressed in E. coli.

•In the stereoselective S-oxidation of methionine, the dioxygenase shows inverse stereopreference to previously characterised hydroxylases.

•The enzyme catalyses the regioselective hydroxylation of several branched-chain amino acids.

•It is a promising catalyst for the synthesis of bioactive compounds and natural product derivatives.

Notes

This project has received funding from the Mercator Research Center Ruhr (Pr-2013-0010) and the European Union's Horizon 2020 MSCA ITN-EID program BIOCASCADES under Grant Agreement No. 634200.

Files

Cloning and characterization of a new delta-specific l-leucine dioxygenase from Anabaena variabilis.pdf

Files (869.2 kB)

Additional details

Related works

References
10.1016/j.jbiotec.2018.07.038 (DOI)

Funding

European Commission
BIOCASCADES - BIOCASCADES- Sustainable and Scalable Biocatalytic Cascade Reactions Training Network 634200