AI Article Synopsis
- Complexity in peptide scaffolds can arise from modifications to ribosomal proteins or from tailored nonribosomal peptides after their initial assembly.
- Nonribosomal peptide synthetase (NRPS) assembly lines, using bimodular and trimodular pathways, work with specific enzymes to efficiently create intricate fungal peptidyl alkaloids in certain fungi.
- The incorporation of the nonproteinogenic amino acid anthranilate as both a starting material and a terminating agent enables the formation of complex peptidyl alkaloid structures with multiple fused rings.
Article Abstract
Complexity generation in naturally occurring peptide scaffolds can occur either by posttranslational modifications of nascent ribosomal proteins or through post assembly line tailoring of nonribosomal peptides. Short enzymatic pathways utilizing bimodular and trimodular nonribosomal peptide synthetase (NRPS) assembly lines, followed by tailoring oxygenases and/or prenyltransferases, efficiently construct complex fungal peptidyl alkaloid scaffolds in Aspergilli, Neosartorya, and Penicillium species. Use of the nonproteinogenic amino acid anthranilate as chain-initiating building block and chain-terminating intramolecular nucleophile leads efficiently to peptidyl alkaloid scaffolds with two to seven fused rings.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3796173 | PMC |
| http://dx.doi.org/10.1021/cb4001684 | DOI Listing |
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