MbtH-like proteins (MLPs) are required for soluble expression and/or optimal activity of some adenylation (A) domains of nonribosomal peptide synthetases (NRPSs). Since A domains can interact with noncognate MLP partners, we investigated how the function of an A domain, TioK, involved in the biosynthesis of the bisintercalator thiocoraline, is altered by noncognate MLPs. Measuring TioK activity with 12 different MLPs from a variety of bacterial species using a radiometric assay suggested that the A domain substrate promiscuity could be altered by foreign MLPs. Kinetic studies and bioinformatics analysis indicated that MLPs’ functions are not as simple as previously thought.
Revised: March 28, 2019 |
Published: October 18, 2018
Citation
Mori S., K.D. Green, R. Choi, G.W. Buchko, M.G. Fried, and S. Garneau-Tsodikova. 2018.Using MbtH-like proteins to alter substrate profile of a nonribosomal peptide adenylation enzyme.Chembiochem 19, no. 20:2186-2194.PNNL-SA-131568.doi:10.1002/cbic.201800240