Premium
Discovery of a Dual Function Cytochrome P450 that Catalyzes Enyne Formation in Cyclohexanoid Terpenoid Biosynthesis
Author(s) -
Chen YuRong,
Naresh Annavareddi,
Liang SuhYuen,
Lin ChunHung,
Chein RongJie,
Lin HsiaoChing
Publication year - 2020
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.202004435
Subject(s) - prenylation , prenyltransferase , enyne , biosynthesis , nonribosomal peptide , natural product , biology , stereochemistry , gene cluster , hevea brasiliensis , cyclase , chemistry , biochemistry , enzyme , gene , organic chemistry , catalysis , natural rubber
The 1,3‐enyne moiety is commonly found in cyclohexanoid natural products produced by endophytic and plant pathogenic fungi. Asperpentyn ( 1 ) is a 1,3‐enyne‐containing cyclohexanoid terpenoid isolated from Aspergillus and Pestalotiopsis . The genetic basis and biochemical mechanism of 1,3‐enyne biosynthesis in 1 , and other natural products containing this motif, has remained enigmatic despite their potential ecological roles. Identified here is the biosynthetic gene cluster and characterization of two crucial enzymes in the biosynthesis of 1 . A P450 monooxygenase that has a dual function, to first catalyze dehydrogenation of the prenyl chain to generate a cis ‐diene intermediate and then serve as an acetylenase to yield an alkyne moiety, and thus the 1,3‐enyne, was discovered. A UbiA prenyltransferase was also characterized and it is unusual in that it favors transferring a five‐carbon prenyl chain, rather than a polyprenyl chain, to a p ‐hydroxybenzoic acid acceptor.