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Biosynthesis of LL‐Z1272β: Discovery of a New Member of NRPS‐like Enzymes for Aryl‐Aldehyde Formation
Author(s) -
Li Chang,
Matsuda Yudai,
Gao Hao,
Hu Dan,
Yao Xin Sheng,
Abe Ikuro
Publication year - 2016
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201600087
Subject(s) - nonribosomal peptide , biosynthesis , prenyltransferase , adenylylation , polyketide synthase , polyketide , gene cluster , enzyme , aldehyde , chemistry , biochemistry , prenylation , stereochemistry , biology , gene , catalysis
LL‐Z1272β ( 1 ) is a prenylated aryl‐aldehyde produced by several fungi; it also serves as a key pathway intermediate for many fungal meroterpenoids. Despite its importance in the biosynthesis of natural products, the molecular basis for the biosynthesis of 1 has yet to be elucidated. Here we identified the biosynthetic gene cluster for 1 from Stachybotrys bisbyi PYH05‐7, and elucidated the biosynthetic route to 1 . The biosynthesis involves a polyketide synthase, a prenyltransferase, and a nonribosomal peptide synthetase (NRPS)‐like enzyme, which is responsible for the generation of the aldehyde functionality. Interestingly, the NRPS‐like enzyme only accepts the farnesylated substrate to catalyze the carboxylate reduction; this represents a new example of a substrate for adenylation domains.