249938-52-1

Usage

Uses

Used in Pharmaceutical Applications:
Kaempferol-7-O-β-D-glucuronide is used as a bioactive compound for its potential health-promoting properties. It is derived from kaempferol, a flavonoid known to have beneficial effects on human health, and the addition of the glucuronide group may enhance its bioavailability and efficacy.
Used in Nutraceutical Applications:
In the nutraceutical industry, kaempferol-7-O-β-D-glucuronide is used as a dietary supplement for its potential health benefits. The compound is derived from natural sources and may contribute to the overall well-being of consumers by providing antioxidant and anti-inflammatory properties.
Used in Cosmetic Applications:
Kaempferol-7-O-β-D-glucuronide is used as an ingredient in the cosmetic industry for its potential skin health benefits. The compound may offer antioxidant protection and contribute to the maintenance of healthy skin by reducing inflammation and promoting skin regeneration.
Used in Functional Food Applications:
In the functional food industry, kaempferol-7-O-β-D-glucuronide is used as an additive for its potential to enhance the health benefits of food products. The compound may provide consumers with additional nutritional value and contribute to the prevention of various health conditions.
Used in Agricultural Applications:
Kaempferol-7-O-β-D-glucuronide can be used in the agricultural industry as a natural compound to improve the health and quality of crops. It may be applied as a supplement to enhance the growth and resistance of plants against various stressors, ultimately leading to higher crop yields and better quality produce.

Upstream product

• 520-18-3 kaempferol 
• 2616-64-0 UDP-glucuronic acid 
• 2616-64-0 uridine diphosphoglucuronic acid 

Relevant academic research and scientific papers

Enzymatic Synthesis of Bioactive O-Glucuronides Using Plant Glucuronosyltransferases

Many O-glucuronides exhibiting various pharmacological activities have been found in nature and in drug metabolism. The glucuronidation of bioactive natural products or drugs to generate glucuronides with better activity and druggability is important in drug discovery and research. In this study, by using two uridine diphosphate (UDP)-dependent glucuronosyltransferases (GATs, UGT88D4 and UGT88D7) from plants, we developed two glucuronidation approaches, pure enzyme catalysis in vitro and recombinant whole-cell catalysis in vivo, to efficiently synthesize bioactive O-glucuronides by the glucuronidation of natural products. In total, 14 O-glucuronides with different structures, including flavonoids, anthraquinones, coumarins, and lignans, were obtained, 7 of which were new compounds. Furthermore, one of the biosynthesized O-glucuronides, kaempferol-7-O-β-d-glucuronide (3a), potently inhibited protein tyrosine phosphatase (PTP) 1B with an IC50 value of 8.02 × 10-6 M. Some of the biosynthesized O-glucuronides also exhibited significant antioxidant activities.

Regioselective glucuronidation of flavonols by six human UGT1A isoforms

Purpose: Glucuronidation is a major barrier to flavonoid bioavailability; understanding its regiospecificity and reaction kinetics would greatly enhance our ability to model and predict flavonoid disposition. We aimed to determine the regioselective glucuronidation of four model flavonols using six expressed human UGT1A isoforms (UGT1A1, 1A3, 1A7, 1A8, 1A9, 1A10). Methods: In vitro reaction kinetic profiles of six UGT1A-mediated metabolism of four flavonols (all with 7-OH group) were characterized; kinetic parameters (Km, Vmax and CLint∈=∈Vmax/Km) were determined. Results: UGT1A1 and 1A3 regioselectively metabolized the 7-OH group, whereas UGT1A7, 1A8, 1A9 and 1A10 preferred to glucuronidate the 3-OH group. UGT1A1 and 1A9 were the most efficient conjugating enzymes with K m values of 1 μM and relative catalytic efficiency ratios of 5.5. Glucuronidation by UGT1As displayed surprisingly strong substrate inhibition. In particular, Ksi values (substrate inhibition constant) were less than 5.4 μM for UGT1A1-mediated metabolism. Conclusion: UGT1A isoforms displayed distinct positional preferences between 3-OH and 7-OH of flavonols. Differentiated kinetic properties between 3-O- and 7-O- glucuronidation suggested that (at least) two distinct binding modes within the catalytic domain were possible. The existence of multiple binding modes should provide better "expert" knowledge to model and predict UGT1A-mediated glucuronidation.