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Using MbtH‐Like Proteins to Alter the Substrate Profile of a Nonribosomal Peptide Adenylation Enzyme
Author(s) -
Mori Shogo,
Green Keith D.,
Choi Ryan,
Buchko Garry W.,
Fried Michael G.,
GarneauTsodikova Sylvie
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800240
Subject(s) - nonribosomal peptide , adenylylation , substrate specificity , enzyme , peptide , substrate (aquarium) , chemistry , biochemistry , biology , biosynthesis , ecology
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.