Substrate and catalytic promiscuity of secondary metabolite enzymes: O-prenylation of hydroxanthone with different prenyl donors by bisinolyl benzoquinone C- and N-prenyltransferase


Prenylated xanthones are secondary metabolites with a broad spectrum of biological activities including antimicrobial and antitumor activities. One xanthone O-prenyltransferase XptB has been identified in Aspergillus nidulans. Recently, we characterised a bisindolyl benzoquinone C- and N-prenyltransferase AstPT from Aspergillus terreus with unusually high substrate specificity towards both the prenyl donor dimethylallyl diphosphate and acceptor bisindolyl benzoquinone. In this study, we demonstrate the acceptance of a number of hydroxyxanthones by AstPT in the presence of not only dimethylallyl but also geranyl and farnesyl diphosphate. Structural elucidation by HR-MS and NMR analyses proved the O-prenylation of all thirteen isolated enzyme products with different prenyl moieties. These results demonstrated the remarkable substrate and catalytic promiscuity of AstPT, which was recognised as a specific enzyme prior to this study.


Sylwia Tarcz, Xiulan Xieb, Shu-Ming Li


RSC Advances

Year, Volume, Page

2014, 4, 17986



Tag Element Regiochemistry Product Substrate Cofactor Enzyme
PTDBREC00224 O Regular AstPT
PTDBREC00225 O Regular AstPT
PTDBREC00226 O Regular AstPT
PTDBREC00227 O Regular AstPT
PTDBREC00228 O Regular AstPT
PTDBREC00229 O Regular AstPT
PTDBREC00230 O Regular AstPT
PTDBREC00231 O Regular AstPT
PTDBREC00232 O Regular AstPT
PTDBREC00233 O Regular AstPT
PTDBREC00234 O Regular AstPT
PTDBREC00235 O Regular AstPT
PTDBREC00236 O Regular AstPT