Journal
BIOCHEMISTRY
Volume 49, Issue 46, Pages 9946-9947Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi101539b
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Funding
- National Institutes of Health [GM49338, F32GM083464]
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Nonribosomal peptide synthetase (NRPS) assembly lines are major avenues for the biosynthesis of a vast array of peptidyl natural products. Several hundred bacterial NRPS gene clusters contain a small (similar to 70-residue) protein belonging to the MbtH family for which no function has been defined. Here we show that two strictly conserved Trp residues in MbtH-like proteins contribute to stimulation of amino acid adenylation in some NRPS modules. We also demonstrate that adenylation can be stimulated not only by cognate MbtH-like proteins but also by homologues from disparate natural product pathways.
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