title: Type II thioesterase restores activity of a NRPS module stalled with an aminoacyl-S-enzyme that cannot be elongated.
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
authors.forename: Ellen
authors.initials: E
authors.lastname: Yeh
authors.forename: Rahul M
authors.initials: RM
authors.lastname: Kohli
authors.forename: Steven D
authors.initials: SD
authors.lastname: Bruner
authors.forename: Christopher T
authors.initials: CT
authors.lastname: Walsh
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D000619:Aminohydrolases / Q000378:metabolism*; D003543:Cysteamine / Q000737:chemistry / Q000378:metabolism; D064429:Fatty Acid Synthases / Q000378:metabolism*; D006868:Hydrolysis; D010453:Peptide Synthases / Q000378:metabolism*; D013869:Thiolester Hydrolases / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D003543:Cysteamine; D064429:Fatty Acid Synthases; D013869:Thiolester Hydrolases; C022738:thioesterase II; D000619:Aminohydrolases; D010453:Peptide Synthases; C104385:non-ribosomal peptide synthase