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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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Publication details

The article was received on 21 Aug 2018, accepted on 08 Oct 2018 and first published on 10 Oct 2018


Article type: Communication
DOI: 10.1039/C8OB02054J
Citation: Org. Biomol. Chem., 2018, Advance Article
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    Identification of a lysine 4-hydroxylase from the glidobactin biosynthesis and evaluation of its biocatalytic potential

    A. Amatuni and H. Renata, Org. Biomol. Chem., 2018, Advance Article , DOI: 10.1039/C8OB02054J

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