71484-85-0

Usage

Uses

Used in Biochemical Research:
4-Nitrophenyl alpha-D-Glucuronide is used as a substrate for beta-glucuronidase enzyme assays to detect and quantitate the enzyme's activity. This is essential for understanding the enzyme's role in various biological processes.
Used in Pharmaceutical Applications:
In the pharmaceutical industry, 4-Nitrophenyl alpha-D-Glucuronide is used to study the metabolic pathway of glucuronidation, an important phase II detoxification process. This helps in the development of drugs and understanding their metabolism and potential toxicity.
Used in Drug Metabolism and Toxicology:
4-Nitrophenyl alpha-D-Glucuronide is used as a tool to investigate the conjugation and detoxification processes in the body. This is vital for assessing the safety and efficacy of drugs and their potential side effects.
Used in the Study of Metabolic Pathways:
4-Nitrophenyl alpha-D-Glucuronide is employed to explore the glucuronidation pathway, which is a key component of the body's detoxification system. Understanding this pathway is crucial for developing treatments and managing diseases related to detoxification processes.

InChI:InChI=1/C12H13NO9/c14-7-8(15)10(11(17)18)22-12(9(7)16)21-6-3-1-5(2-4-6)13(19)20/h1-4,7-10,12,14-16H,(H,17,18)/t7-,8-,9-,10+,12-/m0/s1

Upstream product

• 3767-28-0 4-nitrophenyl-α-D-glucopyranoside 
• 100-02-7 4-nitro-phenol 
• 63700-19-6 uridine-5'-diphospho-α-D-glucuronic acid trisodium salt 

Downstream Products

• 6556-12-3 D-glucuronic acid 

Relevant academic research and scientific papers

DNA-catalyzed glycosylation using aryl glycoside donors

We report the identification by in vitro selection of Zn2+/Mn2+-dependent deoxyribozymes that glycosylate the 3′-OH of a DNA oligonucleotide. Both β and α anomers of aryl glycosides can be used as the glycosyl donors. Individual deox

Purification and characterization of a novel α-glucuronidase from Aspergillus niger specific for O-α-D-glucosyluronic acid α-D-glucosiduronic acid

A new α-glucuronidase that specifically hydrolyzed O-α-D-glucosyluronic acid α-D-glucosiduronic acid (trehalose dicarboxylate, TreDC) was purified from a commercial enzyme preparation from Aspergillus niger, and its properties were examined. The enzyme did not degrade O-α-D-glucosyluronic acid α-D-glucoside, O-α-D-glucosyluronic acid β-D-glucosiduronic acid, O-α-D-glucosyluronic acid-(1 → 2)-β-D-fructosiduronic acid, p-nitrophenyl-O-α-D-glucosiduronic acid, methyl-O-α-D-glucosiduronic acid, or 6-O-α-(4-O-α-D- glucosyluronic acid)-D-glucosyl-β-cyclodextrine. Furthermore, it showed no activity on α-glucuronyl linkages of 4-O-methyl-D-glucosyluronic acid-α-(1 → 2)-xylooligosaccharides, derived from xylan, a supposed substrate of α-glucuronidases. The molecular mass of the enzyme was estimated to be 120 kDa by gel filtration and 58 kDa by SDS-PAGE suggesting, the enzyme is composed of two identical subunits. It was most active at pH 3.0-3.5 and at 40°C. It was stable in pH 2.0-4.5 and below 30°C. It hydrolyzed O-α-D-glucosyluronic acid α-D-glucosiduronic acid to produce α- and β-anomers of D-glucuronic acid in an equimolar ratio. This result suggests that inversion of the anomeric configuration of the substrate is involved in the hydrolysis mechanism.

Enzymic synthesis of β-glucuronides of estradiol, ethynylestradiol and other phenolic substrates on a preparative scale employing UDP-glucuronyl transferase

By incubation of bovine liver UDP-glucuronyl transferase with various phenolic aglycone substrates, preparation of the corresponding β-glucuronides could be achieved in milligram quantities. Concomitantly, simple access was generated to estrogen steroid glucuronides of great biological importance. In terms of experimental feasibility, direct application of the commercially available crude microsomal product was compared to and proven to be competitive with the usually preferred utilization of an immobilized enzyme preparation.