Cysteine is a vital amino acid with wide biological utility, serving functions in catalysis, ligand binding, and maintenance of protein structures. In a subset of natural products, termed ribosomally synthesized and post-translationally modified peptides (RiPPs), multiple subclasses are defined by the enzymatic modific...
Emily M. Dieter, A. Woodard, J. Green et al.· ACS Bio & Med Chem Au· 0 citations
Cytochrome P450s catalyze an array of reactions including crosslinking of aromatic side chains in the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs). ApyO is a cytochrome P450 that forms a C─C bond between two tyrosines in a YLY motif in the substrate ApyA, the precursor pept...
Chandrashekhar Padhi, Dinh T. Nguyen, Ling-Yang Zhu et al.· Angewandte Chemie· 1 citation
Influenza A virus continues to pose pandemic threats, as demonstrated by the recent global spread of highly pathogenic H5N1 strains. Consequently, the development and characterization of vaccines targeting zoonotic influenza subtypes have become a major focus of the field. In this study, we characterize two broadly rea...
Guthrie L. Stroh, Hui-Bin Lv, Chun-Ke Chen et al.· bioRxiv· 0 citations
Isoaspartate (isoAsp) formation is typically viewed as a “molecular clock” through nonenzymatic degradation of aspartate or asparagine during protein aging. Here we report a nearly universal enzymatic pathway for the formation of a conserved isoAsp in the bacterial ribosomal protein uS11. Proteome-wide protein-protein...
Yan-Qing Xue, Chandrima Majumdar, Salimat O. Sofela et al.· bioRxiv· 0 citations
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