The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458, USA.
Org Biomol Chem. 2019 Feb 13;17(7):1736-1739. doi: 10.1039/c8ob02054j.
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.
我们介绍了 GlbB 的功能特征，它是来自 glidobactin 生物合成基因簇的赖氨酸 4-羟化酶。尽管其底物特异性狭窄，但 GlbB 能够以优异的总周转数和完全的区域和立体选择性催化 l-赖氨酸的羟化。GlbB 的合成实用性通过其在 glidobactin 的关键二肽片段的高效制备中的应用得到了说明。
