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Activation of the pacidamycin PacL adenylation domain by MbtH-like proteins.


ABSTRACT: Nonribosomal peptide synthetase (NRPS) assembly lines are major avenues for the biosynthesis of a vast array of peptidyl natural products. Several hundred bacterial NRPS gene clusters contain a small (?70-residue) protein belonging to the MbtH family for which no function has been defined. Here we show that two strictly conserved Trp residues in MbtH-like proteins contribute to stimulation of amino acid adenylation in some NRPS modules. We also demonstrate that adenylation can be stimulated not only by cognate MbtH-like proteins but also by homologues from disparate natural product pathways.

SUBMITTER: Zhang W 

PROVIDER: S-EPMC2982891 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature

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Activation of the pacidamycin PacL adenylation domain by MbtH-like proteins.

Zhang Wenjun W   Heemstra John R JR   Walsh Christopher T CT   Imker Heidi J HJ  

Biochemistry 20101101 46


Nonribosomal peptide synthetase (NRPS) assembly lines are major avenues for the biosynthesis of a vast array of peptidyl natural products. Several hundred bacterial NRPS gene clusters contain a small (∼70-residue) protein belonging to the MbtH family for which no function has been defined. Here we show that two strictly conserved Trp residues in MbtH-like proteins contribute to stimulation of amino acid adenylation in some NRPS modules. We also demonstrate that adenylation can be stimulated not  ...[more]

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