Using MbtH-Like Proteins to Alter the Substrate Profile of a Nonribosomal Peptide Adenylation Enzyme

Shogo Mori, Keith D. Green, Ryan Choi, Garry W. Buchko, Michael G. Fried, Sylvie Garneau-Tsodikova

Research output: Contribution to journalArticle

9 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)2186-2194
Number of pages9
JournalChemBioChem
Volume19
Issue number20
DOIs
StatePublished - Oct 18 2018
Externally publishedYes

Keywords

  • bioinformatics
  • biosynthesis
  • enzymes
  • kinetics
  • protein–protein interactions

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Using MbtH-Like Proteins to Alter the Substrate Profile of a Nonribosomal Peptide Adenylation Enzyme'. Together they form a unique fingerprint.

Cite this