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Title of Journal: Biotechnol Lett

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Abbravation: Biotechnology Letters

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Springer Netherlands

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DOI

10.1007/bf00361858

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1573-6776

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Sitedirected modification of the adenylation doma

Authors: Jae Woo Han Eun Young Kim Jung Min Lee Yun Sung Kim Eunjung Bang Beom Seok Kim
Publish Date: 2012/03/27
Volume: 34, Issue: 7, Pages: 1327-1334
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Abstract

Fusaricidins produced by Paenibacillus polymyxa DBB1709 are lipopeptide antibiotics active against fungi and Grampositive bacteria The cyclic hexapeptide structures of fusaricidins are synthesized by fusaricidin synthetase a nonribosomal peptide synthetase The adenylation domain of the third module FusAA3 can recruit lTyr lVal lIle lalloIle or lPhe which diversifies the fusaricidin structures Since the lPheincorporated fusaricidin analog LIF07 exhibits more potent antimicrobial activity than other analogs we modified a specificityconferring sequence in the substrate binding pocket of FusAA3 to direct the enhanced production of LIF07 Base on comparison to the adenylation domain of gramicidin S synthetase 1 and tyrocidine synthetase 1 both of which mainly activate lPhe six mutant strains with altered FusAA3 were generated using sitedirected mutagenesis M3 I239W I299V M5 I299V G322A V330I and M6 S239W I299V G322A V330I mutants produced significantly more LIF07 than the wildtype strain

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