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.

中文翻译：

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从glidobactin生物合成中鉴定赖氨酸4-羟化酶并评估其生物催化潜力。

我们目前的功能表征GlbB，从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，但是GlbB能够以优异的总周转数以及完全的区域和非对映选择性催化L-赖氨酸的羟基化。GlbB在有效制备格列葡汀的关键二肽片段中的应用说明了GlbB的合成效用。