ArticleSynthetic and systems biotechnology2022
Translocation of subunit PPSE in plipastatin synthase and synthesis of novel lipopeptides.
Article in Synthetic and systems biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 9 citations in OpenAlex.
- Structural Basis for a Scaffolding Role of the COM Domain in Nonribosomal Peptide Synthetases.Angewandte Chemie (International ed. in English) · 2025Article
- Structure, Function and Engineering of the Nonribosomal Peptide Synthetase Condensation Domain.International journal of molecular sciences · 2024Review
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7 authors at 2 institutions in 1 country.
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Abstract
Nonribosomal peptide synthase (NRPS) is a unique molecular assembly mechanism with high hybridity. Its recombination is conducive to the development of novel lipopeptides. However, there are few reports on NRPS subunit recombination of plipastatin at present. In this paper, plipastatin synthase was modified by the forward movement of subunit PPSE and the replacement of the communication-mediating (COM) domain. The results showed that ppsABE, a new assembly line, could synthesize novel lipopeptides such as cycle pentapeptide (C
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