Chandrashekhar Padhi

This paper identifies the final steps in fosfazinomycin biosynthesis, revealing an unexpected use of RiPP machinery to assemble phosphonate and hydrazine moieties.

The P450 ApyO crosslinks a 10-residue C-terminal peptide, and substitutions in the YLY motif switch the linkage among C−C, N−C and C−O bonds.

The paper identifies and characterizes a RiPP biosynthetic gene cluster that introduces nitrile groups via an AS-like enzyme, expanding knowledge of RiPP structural diversity and enzymatic versatility.

This study identifies a conserved FHAFRF-motif in precursor peptides of MNIO-encoding BGCs and demonstrates that MNIO and B12-rSAM enzymes catalyze ortho-hydroxylation and crosslinking of phenylalanine residues to form macrocyclic peptides.