Reprogramming Promiscuous Nonribosomal Peptide Synthetases for Production of Specific Peptides.


Journal

Organic letters
ISSN: 1523-7052
Titre abrégé: Org Lett
Pays: United States
ID NLM: 100890393

Informations de publication

Date de publication:
05 04 2019
Historique:
pubmed: 13 3 2019
medline: 20 8 2019
entrez: 13 3 2019
Statut: ppublish

Résumé

Pairs of docking domains (DDs) mediate the selective interations between adjacent nonribosomal peptide synthetases (NRPSs) to form defined protein-protein interactions resulting in defined peptide sequences. New specific rhabdopeptide/xenortide-like peptides (RXPs) were generated by swapping of either flexible or nonfunctional DD pairs between these monomodular RXP-NRPSs against DDs from collinear NRPSs. The results presented a promising means of engineering RXP-producing NRPSs to obtain desired peptides and further substantiated the decisive role of DDs in the NRP synthesis.

Identifiants

pubmed: 30859835
doi: 10.1021/acs.orglett.9b00395
doi:

Substances chimiques

Peptides 0
Peptide Synthases EC 6.3.2.-
non-ribosomal peptide synthase EC 6.3.2.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Pagination

2116-2120

Auteurs

Xiaofeng Cai (X)

Molecular Biotechnology, Department of Biosciences , Goethe University Frankfurt , 60438 Frankfurt am Main , Germany.
School of Pharmacy, Tongji Medical College , Huazhong University of Science and Technology , 430030 Wuhan , China.

Lei Zhao (L)

Molecular Biotechnology, Department of Biosciences , Goethe University Frankfurt , 60438 Frankfurt am Main , Germany.

Helge B Bode (HB)

Molecular Biotechnology, Department of Biosciences , Goethe University Frankfurt , 60438 Frankfurt am Main , Germany.
Buchmann Institute for Molecular Life Sciences (BMLS) , Goethe University Frankfurt , 60438 Frankfurt am Main , Germany.

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Classifications MeSH