Identification of a Lysine 4-hydroxylase from the Glidobactin Biosynthesis and Evaluation of Its Biocatalytic Potential

Overview

Journal Org Biomol Chem

Publisher Royal Society of Chemistry

Specialties Biochemistry
Chemistry

Date 2018 Oct 16

PMID 30320324

Citations 19

Authors

Alexander Amatuni

Hans Renata

Affiliations

Soon will be listed here.

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.

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