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. 2019 Jun 13;15:1298–1303. doi: 10.3762/bjoc.15.128

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Copyright © 2019, Diettrich et al.

This is an Open Access article under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0). Please note that the reuse, redistribution and reproduction in particular requires that the authors and source are credited.

The license is subject to the Beilstein Journal of Organic Chemistry terms and conditions: (https://www.beilstein-journals.org/bjoc/terms)

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A) Organization of the micacocidin-type gene cluster from Massilia sp. NR 4-1 (top) and of the mic gene cluster from R. solanacearum GMI1000 (bottom). The open reading frames are color-coded according to their predicted function. B) Domain architecture of the massiliachelin (top) and the micacocidin (bottom) assembly lines. Domain notation: FAAL, fatty acyl-AMP ligase; ACP, acyl carrier protein; KS, β-ketoacyl synthase; AT, acyltransferase; KR, ketoreductase; C, condensation; A, adenylation; MT, methyltransferase; PCP, peptidyl carrier protein; TE, thioesterase. The asterisk indicates a methyltransferase-like epimerization domain. C) UV chromatograms of crude culture extracts from Massilia sp. NR 4-1 grown under iron-deficient (top) and iron-replete (bottom) conditions. The chromatograms were recorded at a wavelength of 274 nm.