| Literature DB >> 30134012 |
Shogo Mori1, Keith D Green1, Ryan Choi2,3, Garry W Buchko3,4,5, Michael G Fried6, Sylvie Garneau-Tsodikova1.
Abstract
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.Entities:
Keywords: bioinformatics; biosynthesis; enzymes; kinetics; protein-protein interactions
Mesh:
Substances:
Year: 2018 PMID: 30134012 PMCID: PMC6439349 DOI: 10.1002/cbic.201800240
Source DB: PubMed Journal: Chembiochem ISSN: 1439-4227 Impact factor: 3.164