Ontology highlight
ABSTRACT:
SUBMITTER: Felnagle EA
PROVIDER: S-EPMC2974439 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
Felnagle Elizabeth A EA Barkei John J JJ Park Hyunjun H Podevels Angela M AM McMahon Matthew D MD Drott Donald W DW Thomas Michael G MG
Biochemistry 20101001 41
The biosynthesis of many natural products of clinical interest involves large, multidomain enzymes called nonribosomal peptide synthetases (NRPSs). In bacteria, many of the gene clusters coding for NRPSs also code for a member of the MbtH-like protein superfamily, which are small proteins of unknown function. Using MbtH-like proteins from three separate NRPS systems, we show that these proteins copurify with the NRPSs and influence amino acid activation. As a consequence, MbtH-like proteins are ...[more]