Title of article :
Prenylation of tyrosine and derivatives by a tryptophan C7-prenyltransferase
Author/Authors :
Fan، نويسنده , , Aili and Li، نويسنده , , Shu-Ming، نويسنده ,
Issue Information :
هفته نامه با شماره پیاپی سال 2014
Abstract :
7-DMATS from Aspergillus fumigatus and SirD from Leptosphaeria maculans catalyse a C7-prenylation of l-tryptophan and an O-prenylation of l-tyrosine in nature, respectively. SirD was reported to catalyse the C7-prenylation of l-tryptophan and some derivatives thereof in vitro. We report here the O-prenylation of tyrosine and O- or N-prenylation of its derivatives by 7-DMATS. These results provide experimental evidence for the close relationship of tyrosine O- and tryptophan C7-prenyltransferases regarding their substrate and catalytic promiscuity.
Keywords :
Tyrosine prenylation , substrate promiscuity , Tryptophan prenyltransferase , enzyme catalysis , catalytic promiscuity
Journal title :
Tetrahedron Letters
Journal title :
Tetrahedron Letters