This website uses cookies to give you the best user experience. If you continue without changing your settings we'll assume you are happy to receive all RSC cookies. You can change your cookie settings by navigating to our Privacy and Cookies page and following the instructions. These instructions are also obtainable from the privacy link at the bottom of any RSC page.
Lite Version|Standard version
Home > Organic & Biomolecular ... >
To gain access to this content please
Log in via your home Institution.
Log in with your member or subscriber username and password.
Download


Buy PDF Add PDF to Basket (£42.50*)
*Exclusive of taxes
This article contains 4 page(s)
Abstract | Cited by

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

Page: ^ Top


Enter Keywords, author, title,reference, or DOI
Log in | Register