| 1 |
C7-prenylation of tryptophanyl and O-prenylation of tyrosyl residues in dipeptides by an Aspergillus terreus prenyltransferase
Wunsch C, Zou HX, Linne U, Li SM
Applied Microbiology and Biotechnology, 99(4), 1719, 2015 |
| 2 |
Tyrosine O-prenyltransferases TyrPT and SirD displaying similar behavior toward unnatural alkyl or benzyl diphosphate as their natural prenyl donor dimethylallyl diphosphate
Yu HL, Liebhold M, Xie XL, Li SM
Applied Microbiology and Biotechnology, 99(17), 7115, 2015 |
| 3 |
A promiscuous prenyltransferase from Aspergillus oryzae catalyses C-prenylations of hydroxynaphthalenes in the presence of different prenyl donors
Pockrandt D, Sack C, Kosiol T, Li SM
Applied Microbiology and Biotechnology, 98(11), 4987, 2014 |
| 4 |
A new member of the DMATS superfamily from Aspergillus niger catalyzes prenylations of both tyrosine and tryptophan derivatives
Fan AL, Chen HZ, Wu R, Xu H, Li SM
Applied Microbiology and Biotechnology, 98(24), 10119, 2014 |
| 5 |
Identification of a brevianamide F reverse prenyltransferase BrePT from Aspergillus versicolor with a broad substrate specificity towards tryptophan-containing cyclic dipeptides
Yin SQ, Yu X, Wang Q, Liu XQ, Li SM
Applied Microbiology and Biotechnology, 97(4), 1649, 2013 |
| 6 |
Substrate promiscuity of secondary metabolite enzymes: prenylation of hydroxynaphthalenes by fungal indole prenyltransferases
Yu X, Xie XL, Li SM
Applied Microbiology and Biotechnology, 92(4), 737, 2011 |
