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Issue 7, 2019
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Identification of a lysine 4-hydroxylase from the glidobactin biosynthesis and evaluation of its biocatalytic potential

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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

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Supplementary files

Article information


Submitted
21 Aug 2018
Accepted
08 Oct 2018
First published
10 Oct 2018

Org. Biomol. Chem., 2019,17, 1736-1739
Article type
Communication

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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