Substrate promiscuity of the cyclic dipeptide prenyltransferases from Aspergillus fumigatus ( section sign).
This study reports that a series of tryptophan derivatives with modifications on the side chain or at the indole ring were accepted by two cyclic dipeptide prenyltransferases, CdpNPT and FtmPT1, and converted to prenylated derivatives. The structures of the enzymatic products were elucidated by NMR and MS analyses. In comparison to cyclic dipeptides, which were reversely prenylated by CdpNPT at N-1 and in a regular manner by FtmPT1 at C-2, respectively, tryptophan and its simple derivatives were prenylated reversely by both enzymes at N-1. These results demonstrated the substrate promiscuity of both enzymes.
Zou
Huixi
H
Institut fur Pharmazeutische Biologie, Philipps-Universitat Marburg, Deutschhausstrasse 17A, D-35037 Marburg, Germany.
Zheng
Xiaodong
X
Li
Shu-Ming
SM
D001232:Aspergillus fumigatus / Q000201:enzymology* / Q000378:metabolism; D004122:Dimethylallyltranstransferase / Q000737:chemistry / Q000378:metabolism*; D004151:Dipeptides / Q000737:chemistry; D015394:Molecular Structure; D013379:Substrate Specificity; D014364:Tryptophan / Q000031:analogs & derivatives* / Q000737:chemistry*
D004151:Dipeptides; C029951:tryptophyltyrosine; D014364:Tryptophan; C534855:CdpNPT protein, Aspergillus fumigatus; D004122:Dimethylallyltranstransferase; C534854:FtmPT1 protein, Aspergillus fumigatus