Issue 7, 2019

Identification of a lysine 4-hydroxylase from the glidobactin biosynthesis and evaluation of its biocatalytic potential

Abstract

We present the functional characterization of GlbB, a lysine 4-hydroxylase from the glidobactin biosynthetic gene cluster. Despite its narrow substrate specificity, GlbB is able to catalyze the hydroxylation of L-lysine with excellent total turnover number and complete regio- and diastereoselectivity. The synthetic utility of GlbB is illustrated by its use in the efficient preparation of a key dipeptide fragment of glidobactin.

Graphical abstract: Identification of a lysine 4-hydroxylase from the glidobactin biosynthesis and evaluation of its biocatalytic potential

Supplementary files

Article information

Article type
Communication
Submitted
21 ago. 2018
Accepted
08 oct. 2018
First published
10 oct. 2018

Org. Biomol. Chem., 2019,17, 1736-1739

Identification of a lysine 4-hydroxylase from the glidobactin biosynthesis and evaluation of its biocatalytic potential

A. Amatuni and H. Renata, Org. Biomol. Chem., 2019, 17, 1736 DOI: 10.1039/C8OB02054J

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