117153-55-6

Usage

Uses

Used in Biochemical Research:
4-(TRIFLUOROMETHYL)UMBELLIFERYL-BETA-D-GALACTOPYRANOSIDE is used as a fluorogenic substrate for the detection and quantification of beta-galactosidase activity. The trifluoromethyl group increases the compound's fluorescence, allowing for the accurate measurement of enzyme activity in various biological samples.
Used in Medical Research:
In the medical field, 4-(TRIFLUOROMETHYL)UMBELLIFERYL-BETA-D-GALACTOPYRANOSIDE is utilized as a diagnostic tool for studying the activity of beta-galactosidase, which is an important enzyme in the metabolism of lactose and other substrates. 4-(TRIFLUOROMETHYL)UMBELLIFERYL-BETA-D-GALACTOPYRANOSIDE's fluorescence properties enable researchers to monitor enzyme activity in clinical samples, aiding in the diagnosis and understanding of various medical conditions related to enzyme function.
Used in Drug Development:
4-(TRIFLUOROMETHYL)UMBELLIFERYL-BETA-D-GALACTOPYRANOSIDE can be employed in the development of drugs targeting beta-galactosidase or related enzymes. Its ability to produce a fluorescent product upon enzyme action allows for the assessment of drug efficacy and the optimization of drug candidates that modulate beta-galactosidase activity.
Used in Analytical Chemistry:
In analytical chemistry, 4-(TRIFLUOROMETHYL)UMBELLIFERYL-BETA-D-GALACTOPYRANOSIDE serves as a sensitive and selective probe for the detection of beta-galactosidase activity. Its fluorescence properties enable the development of assays and methods for the precise measurement of enzyme activity, which can be applied in various analytical techniques such as high-performance liquid chromatography (HPLC) and fluorescence spectroscopy.

InChI:InChI=1/C16H15F3O8/c17-16(18,19)8-4-11(21)26-9-3-6(1-2-7(8)9)25-15-14(24)13(23)12(22)10(5-20)27-15/h1-4,10,12-15,20,22-24H,5H2/t10-,12+,13+,14-,15-/m1/s1

Upstream product

• 575-03-1 7-hydroxy-4-(trifluoromethyl)-2H-chromen-2-one 
• 572-09-8 2,3,4,6-tetra-O-acetyl-α-D-glucopyranosyl bromide 

Relevant academic research and scientific papers

Glycosyl Cations versus Allylic Cations in Spontaneous and Enzymatic Hydrolysis

Enzymatic prenyl and glycosyl transfer are seemingly unrelated reactions that yield molecules and protein modifications with disparate biological functions. However, both reactions employ diphosphate-activated donors and each proceed via cationic species: allylic cations and oxocarbenium ions, respectively. In this study, we explore the relationship between these processes by preparing valienyl ethers to serve as glycoside mimics that are capable of allylic rather than oxocarbenium cation stabilization. Rate constants for spontaneous hydrolysis of aryl glycosides and their analogous valienyl ethers were found to be almost identical, as were the corresponding activation enthalpies and entropies. This close similarity extended to the associated secondary kinetic isotope effects (KIEs), indicating very similar transition state stabilities and structures. Screening a library of over 100 β-glucosidases identified a number of enzymes that catalyze hydrolysis of these valienyl ethers with kcat values up to 20 s-1. Detailed analysis of one such enzyme showed that ether hydrolysis occurs via the analogous mechanisms found for glycosides, and through a very similar transition state. This suggests that the generally lower rates of enzymatic cleavage of the cyclitol ethers reflects evolutionary specialization of these enzymes toward glycosides rather than inherent reactivity differences.

USE OF COUMARIN DERIVATIVES IN ANTIFUNGAL THERAPY

The invention provides coumarin compounds, in particular glycosidic coumarin compounds, useful in the treatment of dermatophyte fungal infections.