title: Carbon extension in peptidylnucleoside biosynthesis by radical SAM enzymes.
abstract: Nikkomycins and polyoxins are antifungal peptidylnucleoside antibiotics active against human and plant pathogens. Here we report that during peptidylnucleoside biosynthesis in Streptomyces cacaoi and S. tendae, the C5' extension of the nucleoside essential for downstream structural diversification is catalyzed by a conserved radical S-adenosyl-L-methionine (SAM) enzyme, PolH or NikJ. This is distinct from the nucleophilic mechanism reported for antibacterial nucleosides and represents a new mechanism of nucleoside natural product biosynthesis.
authors.affiliation: Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, USA.
authors.forename: Edward A
authors.initials: EA
authors.lastname: Lilla
authors.affiliation: Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, USA.|Department of Chemistry, Duke University, Durham, North Carolina, USA.
authors.forename: Kenichi
authors.initials: K
authors.lastname: Yokoyama
mesh_terms: D002244:Carbon / Q000737:chemistry / Q000378:metabolism*; D005609:Free Radicals / Q000737:chemistry / Q000378:metabolism; D008968:Molecular Conformation; D009705:Nucleosides / Q000096:biosynthesis* / Q000737:chemistry; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011496:Protein Methyltransferases / Q000737:chemistry / Q000378:metabolism*; D012436:S-Adenosylmethionine / Q000737:chemistry / Q000378:metabolism; D013302:Streptomyces / Q000737:chemistry / Q000378:metabolism
chemical_list: D005609:Free Radicals; D009705:Nucleosides; D010455:Peptides; D002244:Carbon; D012436:S-Adenosylmethionine; D011496:Protein Methyltransferases