Identification of a lysine 4-hydroxylase from the glidobactin biosynthesis and evaluation of its biocatalytic potential
Identification of a lysine 4-hydroxylase from the glidobactin biosynthesis and evaluation of its biocatalytic potential
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DOI：
10.1039/c8ob02054j
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发表时间：
2019-02-21
影响因子：
3.2
通讯作者：
Renata, Hans
中科院分区：
文献类型：
--
作者：
Amatuni, Alexander;Renata, Hans
我们提出了GlbB，赖氨酸4-羟化酶从glidobactin生物合成基因簇的功能特性。尽管其狭窄的底物特异性，GlbB能够催化L-赖氨酸的羟基化，具有优异的总周转数和完全的区域和非对映选择性。GlbB的合成效用通过其在有效制备格列菌素的关键二肽片段中的使用来说明。
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.