The tyrosine O-prenyltransferase SirD catalyzes O-, N-, and C-prenylations


Recently, the prenyltransferase SirD was found to be responsible for the O-prenylation of tyrosine in the biosynthesis of sirodesmin PL in Leptosphaeria maculans. In this study, the behavior of SirD towards phenylalanine/tyrosine and tryptophan derivatives was investigated. Product formation has been observed with 12 of 19 phenylalanine/tyrosine derivatives. It was shown that the alanine structure attached to the benzene ring and an electron donor, e.g., OH or NH₂, at its para-position are essential for the enzyme activity. Modifications were possible both at the side chain and the benzene ring. Enzyme products from seven phenylalanine/tyrosine derivatives were isolated and characterized by MS and NMR analyses including HSQC and HMBC and proven to be O- or N-prenylated derivatives at position C4 of the benzene rings. K ( M ) values of six selected derivatives were found in the range of 0.10-0.68 mM. Catalytic efficiencies (K(cat)/K(M)) were determined in the range of 430-1,110 s⁻¹·M⁻¹ with L-tyrosine as the best substrate. In addition, 7 of 14 tested tryptophan analogs were also accepted by SirD and converted to C7-prenylated derivatives, which was confirmed by comparison with products obtained from enzyme assays using a 7-dimethylallyltryptophan synthase 7-DMATS from Aspergillus fumigatus.


Hui-Xi Zou, Xiulan Xie, Xiao-Dong Zheng, Shu-Ming Li


Applied Microbiology and Biotechnology

Year, Volume, Page

2011, 89, 1443



Tag Element Regiochemistry Product Substrate Cofactor Enzyme
PTDBREC00419 O Regular SirD
PTDBREC00420 N Regular SirD
PTDBREC00421 O Regular SirD
PTDBREC00422 O Regular SirD
PTDBREC00423 O Regular SirD
PTDBREC00424 O Regular SirD
PTDBREC00425 O Regular SirD
PTDBREC00426 O Regular SirD
PTDBREC00427 O Regular SirD
PTDBREC00428 O Regular SirD
PTDBREC00429 O Regular SirD
PTDBREC00430 O Regular SirD
PTDBREC00431 O Regular SirD
PTDBREC00432 O Regular SirD
PTDBREC00433 O Regular SirD
PTDBREC00434 O Regular SirD
PTDBREC00435 O Regular SirD
PTDBREC00436 O Regular SirD
PTDBREC00437 O Regular SirD
PTDBREC00438 O Regular SirD
PTDBREC00439 O Regular SirD
PTDBREC00440 O Regular SirD
PTDBREC00441 O Regular SirD
PTDBREC00442 O Regular SirD