The leading module of mycosubtilin: An adenylation domain with fatty acid selectivity

Darren B. Hansen, Stefanie B. Bumpus, Zachary D. Aron, Neil L. Kelleher, Christopher T. Walsh*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

64 Scopus citations


We report the cloning and characterization of the loading domain of mycosubtilin A synthetase responsible for the biosynthesis of mycosubtilin, a lipopeptide natural product from Bacillus subtilis. A truncated form of mycA was cloned and overexpressed and found to activate free fatty acids though an acyl-adenylate intermediate and loaded on the adjacent thiolation domain independently of coenzyme A, contradicting the literature proposal that the loading module is a coenzyme A ligase. The activation and loading of free fatty acids was characterized with a combination of traditional biochemical assays and electrospray ionization-Fourier transform mass spectrometry.

Original languageEnglish (US)
Pages (from-to)6366-6367
Number of pages2
JournalJournal of the American Chemical Society
Issue number20
StatePublished - May 23 2007

ASJC Scopus subject areas

  • General Chemistry
  • Biochemistry
  • Catalysis
  • Colloid and Surface Chemistry


Dive into the research topics of 'The leading module of mycosubtilin: An adenylation domain with fatty acid selectivity'. Together they form a unique fingerprint.

Cite this