Unraveling the Structure and Mechanism of the MST(ery) Enzymes.
Unraveling the Structure and Mechanism of the MST(ery) Enzymes.
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DOI：
10.1016/j.tibs.2018.02.011
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发表时间：
2018-05
影响因子：
13.8
通讯作者：
Lamb AL
中科院分区：
文献类型：
--
作者：
Shelton CL;Lamb AL
The Menaquinone, Siderophore and Tryptophan (MST) enzymes transform chorismate to generate precursor molecules for the biosynthetic pathways defined in their name. Kinetic data, both steady state and transient state, and X-ray crystal structures indicate that these enzymes are highly conserved, both in mechanism and in structure. Because these enzymes are found in pathogens but not humans, there is considerable interest in these enzymes as drug design targets. While great progress has been made in defining enzyme structure and mechanism, inhibitor design has lagged behind. This review provides a detailed description of the evidence that begins to unravel the mystery of how the MST enzymes work, and how that information has been used in inhibitor design.
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