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· 0 citations
Lanthipeptides are one of the largest classes of ribosomally synthesized and post-translationally modified peptides (RiPPs). The coi biosynthetic gene cluster (BGC) from Streptomyces coelicolor A3(2) encodes a canonical class I lanthipeptide dehydratase (CoiB) and cyclase (CoiC), a bifunctional enzyme (CoiSA) with an O...
Jingqi Chen, Ling-Yang Zhu, W. A. van der Donk· bioRxiv· 0 citations
In vitro and in vivo analyses support a recent finding that the defining carbon-carbon bond is formed not by a long-hypothesized PLP-dependent process, but by a vitamin B12-dependent radical SAM enzyme, and expand upon the current knowledge of radical-mediated C-C bond formation and PEARL enzyme catalysis.
Chi-Fang Lee, Tian-Hui H. Zhou, Song-Yi Xue et al.· Journal of the American Chem...· 0 citations
This study uses the ultrahigh-throughput mRNA display technique to map the sequence compatibility of ProcM across a focused library and provides a high-throughput view of ProcM reactivity and highlights differences with previous high-throughput studies on substrate selectivity of RiPP modification enzymes.
Ouyang Yao, Hassan Nadeem, Y. Goto et al.· bioRxiv· 0 citations
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