76754-24-0

Usage

Uses

Used in Pharmaceutical Industry:
3',6-Di(dimethylallyl)genistein is used as a pharmaceutical agent for its anti-inflammatory properties, helping to reduce inflammation in the body and potentially treating inflammatory conditions.
3',6-Di(dimethylallyl)genistein is used as an antioxidant agent for its ability to neutralize free radicals and protect cells from oxidative damage, which may contribute to the prevention of various diseases and aging.
Used in Anticancer Applications:
3',6-Di(dimethylallyl)genistein is used as an anticancer agent for its potential to inhibit the growth and proliferation of cancer cells, making it a candidate for cancer treatment and prevention.
Used in Hormone-Related Conditions:
3',6-Di(dimethylallyl)genistein is used as a modulator of estrogen receptor activity, which may be beneficial for treating hormone-related conditions such as menopause, osteoporosis, and certain types of cancer.
Used in Nutraceutical Industry:
3',6-Di(dimethylallyl)genistein is used as a nutraceutical ingredient for its potential health benefits, including its anti-inflammatory, antioxidant, and anticancer properties, as well as its ability to modulate estrogen receptor activity. It can be incorporated into dietary supplements and functional foods to support overall health and well-being.

Upstream product

• 446-72-0 5,7-Dihydroxy-3-(4-hydroxy-phenyl)-chromen-4-on 
• 780724-90-5 dimethylallyl diphosphate 
• 358-72-5 dimethylallyl diphosphate 
• 1186-30-7 3,3-dimethylallyl diphosphate triammonium salt 

Downstream Products

• 76754-27-3 5-Hydroxy-3-[4-hydroxy-3-(3-methyl-but-2-enyl)-phenyl]-7-methoxy-6-(3-methyl-but-2-enyl)-chromen-4-one 

Relevant academic research and scientific papers

Molecular insights into the enzyme promiscuity of an aromatic prenyltransferase

Aromatic prenyltransferases (aPTases) transfer prenyl moieties from isoprenoid donors to various aromatic acceptors, some of which have the rare property of extreme enzymatic promiscuity toward both a variety of prenyl donors and a large diversity of acceptors. In this study, we discovered a new aPTase, AtaPT, from Aspergillus terreus that exhibits unprecedented promiscuity toward diverse aromatic acceptors and prenyl donors and also yields products with a range of prenylation patterns. Systematic crystallographic studies revealed various discrete conformations for ligand binding with donor-dependent acceptor specificity and multiple binding sites within a spacious hydrophobic substrate-binding pocket. Further structure-guided mutagenesis of active sites at the substrate-binding pocket is responsible for altering the specificity and promiscuity toward substrates and the diversity of product prenylations. Our study reveals the molecular mechanism underlying the promiscuity of AtaPT and suggests an efficient protein engineering strategy to generate new prenylated derivatives in drug discovery applications.

Complementary Flavonoid Prenylations by Fungal Indole Prenyltransferases

Flavonoids are found mainly in plants and exhibit diverse biological and pharmacological activities, which can often be enhanced by prenylations. In plants, such reactions are catalyzed by membrane-bound prenyltransferases. In this study, the prenylation of nine flavonoids from different classes by a soluble fungal prenyltransferase (AnaPT) involved in the biosynthesis of the prenylated indole alkaloid acetylaszonalenin is demonstrated. The behavior of AnaPT toward flavonoids regarding substrate acceptance and prenylation positions clearly differs from that of the indole prenyltransferase 7-DMATS. The two enzymes are therefore complementary in flavonoid prenylations.

Flavanone 8-dimethylallyltransferase in Sophora flavescens cell suspension cultures

Dimethylallyl diphosphate: naringenin 8-dimethylallyltransferase (EC 2.5.1) was characterized. The enzyme was enantiospecific for (-)-(2S)-naringenin and utilized 3,3-dimethylallyl diphosphate as sole prenyl donor. It required Mg2+ (optimum concentration, 10 mM), and has an optimum pH of 9-10. The apparent K(m) values for 3,3-dimethylallyl diphosphate and naringenin were 120 and 36 μM, respectively. The microsomal fraction prenylated several other flavanones at the C-8 position less effectively as compared with naringenin. Interestingly, when 2'-hydroxynaringenin was used as a prenyl acceptor, the 8-lavandulyl (sophoraflavanone G) and the 6-dimethylallyl derivatives were formed, together with the 8-dimethylallyl derivative, leachianone G. These results suggest that the 2'-hydroxy group of naringenin plays an important role for the formation of a lavandulyl group. (C) 2000 Elsevier Science Ltd.