title: Breaking cyclic dipeptide prenyltransferase regioselectivity by unnatural alkyl donors.
abstract: The behavior of five cyclic dipeptide prenyltransferases, responsible for C2-regular, C2-reverse, or C3-reverse prenylation, was investigated in the presence of the unnatural alkyl donors monomethylallyl and 2-pentenyl diphosphate. Both substrates were well accepted by the tested enzymes. Interestingly, C2-reverse and C3-reverse monoalkylated derivatives were identified as enzyme products in all of the enzyme assays. These findings indicate their similar reaction characteristics in the presence of unnatural alkyl donors.
authors.affiliation: Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17a, 35037 Marburg, Germany, and Fachbereich Chemie, Philipps-Universität Marburg, Hans-Meerwein-Strasse, 35032 Marburg, Germany.
authors.forename: Mike
authors.initials: M
authors.lastname: Liebhold
authors.forename: Xiulan
authors.initials: X
authors.lastname: Xie
authors.forename: Shu-Ming
authors.initials: SM
authors.lastname: Li
mesh_terms: D004122:Dimethylallyltranstransferase / Q000737:chemistry* / Q000378:metabolism; D004151:Dipeptides / Q000737:chemistry*; D007211:Indoles / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D009943:Organophosphorus Compounds / Q000737:chemistry; D010456:Peptides, Cyclic / Q000737:chemistry*; D054876:Prenylation; D013379:Substrate Specificity
chemical_list: D004151:Dipeptides; D007211:Indoles; D009943:Organophosphorus Compounds; D010456:Peptides, Cyclic; D004122:Dimethylallyltranstransferase