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

doi:10.1021/ja070890j

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

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

56 Scopus citations

Abstract

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 language	English (US)
Pages (from-to)	6366-6367
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	129
Issue number	20
DOIs	https://doi.org/10.1021/ja070890j
State	Published - May 23 2007

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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abstract = "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.",

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AU - Kelleher, Neil L.

AU - Walsh, Christopher T.

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AB - 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.

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

Abstract

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