Exploring the Post-translational Enzymology of PaaA by mRNA Display
| Autor: | Albert A. Bowers, Steven R Fleming, Yuki Goto, Paul M. Himes, Swapnil V. Ghodge, Hiroaki Suga |
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| Rok vydání: | 2020 |
| Předmět: |
Substrate recognition
Peptide Protein Engineering 010402 general chemistry 01 natural sciences Biochemistry Article Catalysis Substrate Specificity Colloid and Surface Chemistry Bacterial Proteins Point Mutation mRNA display Carbon-Nitrogen Ligases Amino Acid Sequence RNA Messenger Enzyme Assays chemistry.chemical_classification Pantoea Substrate (chemistry) General Chemistry Glutamic acid 0104 chemical sciences Enzyme Post translational chemistry Protein Binding |
| Zdroj: | J Am Chem Soc |
| ISSN: | 1520-5126 0002-7863 |
| Popis: | PaaA is a RiPP enzyme that catalyzes the transformation of two glutamic acid residues within a substrate peptide into the bicyclic core of Pantocin A. Here, for the first time, we use mRNA display techniques to understand RiPP enzyme-substrate interactions to illuminate PaaA substrate recognition. Additionally, our data revealed insights into the enzymatic timing of glutamic acid modification. The technique developed is quite sensitive and a significant advancement over current RiPP studies and opens the door to enzyme modified mRNA display libraries for natural product-like inhibitor pans. |
| Databáze: | OpenAIRE |
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