CmlI is an N-oxygenase in the biosynthesis of chloramphenicol.
CmlI is an N-oxygenase in the biosynthesis of chloramphenicol.
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DOI：
10.1016/j.tet.2012.06.036
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发表时间：
2012-09-16
期刊：
影响因子：
2.1
通讯作者：
Zhao H
中科院分区：
文献类型：
--
作者：
Lu H;Chanco E;Zhao H
The N-oxygenation of an amine group is one of the steps in the biosynthesis of the antibiotic chloramphenicol. The non-heme di-iron enzyme CmlI was identified as the enzyme catalyzing this reaction through bioinformatics studies and reconstitution of enzymatic activity. In vitro reconstitution was achieved using phenazine methosulfate and NADH as electron mediators, while in vivo activity was demonstrated in Escherichia coli using two substrates. Kinetic analysis showed a biphasic behavior of the enzyme. Oxidized hydroxylamine and nitroso compounds in the reaction were detected both in vitro and in vivo based on LC–MS. The active site metal was confirmed to be iron based on a ferrozine assay. These findings provide new insights into the biosynthesis of chloramphenicol and could lead to further development of CmlI as a useful biocatalyst.
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