Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lee T. Todd, Jr. Building, 789 South Limestone St., Lexington, KY, 40536-0596, USA.
University of Washington, Center for Emerging and Re-emerging Infectious Diseases, 750 Republican St., Seattle, WA, 98109, USA.
Chembiochem. 2018 Oct 18;19(20):2186-2194. doi: 10.1002/cbic.201800240. Epub 2018 Oct 4.
MbtH-like proteins (MLPs) are required for soluble expression and/or optimal activity of some adenylation (A) domains of nonribosomal peptide synthetases. Because A domains can interact with noncognate MLP partners, how the function of an A domain, TioK, involved in the biosynthesis of the bisintercalator thiocoraline, is altered by noncognate MLPs has been investigated. Measuring TioK activity with 12 different MLPs from a variety of bacterial species by using a radiometric assay suggested that the A domain substrate promiscuity could be altered by foreign MLPs. Kinetic studies and bioinformatics analysis expanded the complexity of MLP functions and interactions.
MbtH 样蛋白 (MLPs) 是某些非核糖体肽合成酶的腺苷酸化 (A) 结构域可溶性表达和/或最佳活性所必需的。由于 A 结构域可以与非同源的 MLP 伴侣相互作用，因此研究了参与双嵌入剂硫珊瑚素生物合成的 A 结构域 TioK 的功能如何被非同源 MLPs 改变。使用来自多种细菌物种的 12 种不同 MLPs 通过放射性测定法测量 TioK 活性表明，A 结构域底物的混杂性可以被外来 MLPs 改变。动力学研究和生物信息学分析扩展了 MLP 功能和相互作用的复杂性。
