The tyrosine O-prenyltransferase SirD catalyzes O-, N-, and C-prenylations.
Appl Microbiol Biotechnol
; 89(5): 1443-51, 2011 Mar.
Article
in En
| MEDLINE
| ID: mdl-21038099
ABSTRACT
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⻹·M⻹ 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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Aspergillus fumigatus
/
Tyrosine
/
Dimethylallyltranstransferase
/
Prenylation
Language:
En
Journal:
Appl Microbiol Biotechnol
Year:
2011
Document type:
Article