Journal article
A dissected non-ribosomal peptide synthetase maintains activity
Biochimica et biophysica acta. Proteins and proteomics, v 1872(1), pp 140972-140972
01 Jan 2024
PMID: 37951518
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Non-ribosomal peptide synthetases (NRPSs) generate chemically complex compounds and their modular architecture suggests that changing their domain organization can predictably alter their products. Ebony, a small three-domain NRPS, catalyzes the formation of β-alanine containing amides from biogenic amines. To examine the necessity of interdomain interactions, we modeled and docked domains of Ebony to reveal potential interfaces between them. Testing the same domain combinations in vitro showed that 8 % of activity was preserved after Ebony was dissected into a di-domain and a detached C-terminal domain, suggesting that sufficient interaction was maintained after dissection. Our work creates a model to identify domain interfaces necessary for catalysis, an important step toward utilizing Ebony as a combinatorial engineering platform for novel amides.
Metrics
17 Record Views
Details
- Title
- A dissected non-ribosomal peptide synthetase maintains activity
- Creators
- Amanda J Platt - Drexel UniversityShae Padrick - Drexel UniversityAmy T Ma - Drexel UniversityJoris Beld - Drexel University
- Publication Details
- Biochimica et biophysica acta. Proteins and proteomics, v 1872(1), pp 140972-140972
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology; Microbiology and Immunology
- Web of Science ID
- WOS:001165921700001
- Scopus ID
- 2-s2.0-85177481645
- Other Identifier
- 991021811633804721
UN Sustainable Development Goals (SDGs)
This publication has contributed to the advancement of the following goals:
InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics