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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]

PMID: 20964365

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