Literature DB >> 30320324

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

Alexander Amatuni1, Hans Renata.   

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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Year:  2019        PMID： 30320324      PMCID： PMC6374188          DOI： 10.1039/c8ob02054j

Source DB:  PubMed          Journal:  Org Biomol Chem        ISSN： 1477-0520            Impact factor:   3.876


  22 in total

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