17695-46-4

Usage

Uses

Used in Enzyme Assays:
4-METHYLUMBELLIFERYL BUTYRATE is used as a fluorogenic substrate for esterases/lipases, such as butyrate esterase, for the purpose of enzyme activity measurement and analysis. This application is particularly useful in research and diagnostic laboratories to study the function and properties of esterases and lipases.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, 4-METHYLUMBELLIFERYL BUTYRATE is used as a key component in the development of drugs targeting esterases and lipases. Its role as a fluorogenic substrate allows for the assessment of drug efficacy and potential interactions with these enzymes, contributing to the advancement of novel therapeutics.
Used in Research and Development:
4-METHYLUMBELLIFERYL BUTYRATE is employed as a research tool in the field of biochemistry and molecular biology. It is utilized to study the mechanisms of action, substrate specificity, and inhibition of esterases and lipases, providing valuable insights into the structure-function relationships of these enzymes and their role in various biological processes.

InChI:InChI=1/C14H14O4/c1-3-4-13(15)17-10-5-6-11-9(2)7-14(16)18-12(11)8-10/h5-8H,3-4H2,1-2H3

Upstream product

• 90-33-5 7-hydroxy-4-methyl-chromen-2-one 
• 141-75-3 butyryl chloride 
• 106-31-0 butanoic acid anhydride 

Downstream Products

• 90-33-5 7-hydroxy-4-methyl-chromen-2-one 
• 107-92-6 butyric acid 
• 105-54-4 butanoic acid ethyl ester 
• 623-42-7 butanoic acid methyl ester 
• 90104-80-6 8-butyryl-7-hydroxy-4-methyl-coumarin 
• 35031-57-3 1-(2,4-dimethylphenyl)butan-1-one 

Relevant academic research and scientific papers

Anti-influenza drug discovery: Structure-activity relationship and mechanistic insight into novel angelicin derivatives

By using a cell-based high throughput screening campaign, a novel angelicin derivative 6a was identified to inhibit influenza A. (H1N1) virus induced cytopathic effect in Madin-Darby canine kidney cell culture in low micromolar range. Detailed structure-activity relationship studies of 6a revealed that the angelicin scaffold is essential for activity in pharmacophore B, while meta-substituted phenyl/2-thiophene rings are optimal in pharmacophore A and C. The optimized lead 4-methyl-9-phenyl-8-(thiophene-2-carbonyl)-furo[2,3-h] chromen-2-one (8g, IC50 = 70 nM) showed 64-fold enhanced activity compared to the high throughput screening (HTS) hit 6a. Also, 8g was found effective in case of influenza A (H3N2) and influenza B virus strains similar to approved anti-influenza drug zanamivir (4). Preliminary mechanistic studies suggest that these compounds act as anti-influenza agents by inhibiting ribonucleoprotein (RNP) complex associated activity and have the potential to be developed further, which could form the basis for developing additional defense against influenza pandemics.

METHOD FOR DETECTION AND/OR ASSAY OF LOVASTATIN ESTERASE WITH USE OF FLUOROGENIC/CHROMOGENIC REAGENT, LOVASTATIN ESTERASE ISOLATED AND/OR PURIFIED BY THIS METHOD, ASSEMBLY FOR DETECTION AND/OR ASSAY AND USE OF FLUOROGENIC/CHROMOGENIC REAGENT FOR DETECTION AND/OR ASSAY OF LOVASTATIN ESTERASE

The invention relates to a method for detection and/or assay of the lovastatin esterase enzymatic activity, with use of the fiuorogenic/chromogenic reagent, comprising use of the fiuorogenic/chromogenic reagent of formula II wherein R represents hydrogen or C1-C6-alkyl, R' represents one or two substituents of the ring A, R" represents one or two or three substituents of the ring B. According to a method, the reagent is added to a material of enzymatic activity and the hydrolysis reaction under enzyme action is carried out, followed by detection and/or assay of the liberated coumarin compound of formula III. Also the invention relates to lovastatin esterase isolated and/or purified using this method, an assembly for detection and/or assay of the lovastatin esterase enzymatic activity, an use of the fiuorogenic/chromogenic reagent of formula II for detection and/or assay of the lovastatin esterase enzymatic activity.

Structure activity studies with xenobiotic substrates using carboxylesterases isolated from Arabidopsis thaliana

Carboxylesterases (CXEs) catalyse the hydrolysis of xenobiotics and natural products radically altering their biological activities. Whereas the substrate selectivity of animal CXEs, such as porcine liver esterase (PLE) have been well studied, the respective enzymes in plants have yet to be defined and their activities determined. Using Arabidopsis thaliana (At) as a source, five representative members of the α/β hydrolase AtCXE family of proteins have been cloned, expressed and the purified recombinant proteins assayed for esterase activity with xenobiotic substrates. Two members, AtCXE5 and AtCXE18 were found to be active carboxylesterases, though AtCXE5 proved to be highly unstable as a soluble protein. AtCXE18 and the previously characterised S-formylglutathione hydrolase from Arabidopsis (AtSFGH) were assayed against a series of esters based on methylumbelliferone in which the acyl moiety was varied with respect to size and conformation. The same series was used to assay crude esterase preparation from Arabidopsis plants and the results compared with those obtained with the commonly used PLE. With straight chain esters, AtCXE18 behaved like PLE, but the Arabidopsis hydrolases proved less tolerant of branched chain acyl components than the mammalian enzyme. While none of the enzyme preparations accurately reflected all the activities determined with crude Arabidopsis protein extracts, the plant enzymes proved more useful than PLE in predicting the hydrolysis of the more sterically constrained esters.

A high-throughput, low-volume enzyme assay on solid support

A high-throughput enzyme assay is described that uses 1 μL or less of enzyme solution for each test Enzyme solutions are deposited by robotic handling in a throughput of over 1000 tests/h on the surface of silica gel plates that have been preimpregnated with fluorogenic substrates. The reaction is quantitated by fluorescence. The method is compatible with water-insoluble substrates (lipases), water-soluble substrates (glycosidases), whole-protein substrates (proteases), and enzyme inhibition measurements. Hydrolytically labile umbelliferyl esters can be used to assay lipases in this format without background hydrolysis. High throughput and reproducibility were tested by fingerprint analysis of lipases and esterases against 37 different fluorogenic ester substrates. A set of eight fluorogenic unbelliferyl esters was selected for optimal activity screening of lipases and esterases on silica gel plates.

Synthesis, characterization and in vitro anti-invasive activity screening of polyphenolic and heterocyclic compounds

Invasion is the hallmark of malignant tumors, and is responsible for the bad prognosis of the untreated cancer patients. The search for anti-invasive treatments led us to screen compounds of different classes for their effect in an assay for invasion. Thirty-nine new compounds synthesized in the present study along with 56 already reported compounds belonging mainly to the classes of lactones, pyrazoles, isoxazoles, coumarins, desoxybenzoins, aromatic ketones, chalcones, chromans, isoflavanones have been tested against organotypic confronting cultures of invasive human MCF-7/6 mammary carcinoma cells with embryonic chick heart fragments in vitro. Three of them (a pyrazole derivative, an isoxazolylcoumarin and a prenylated desoxybenzoin) inhibited invasion at concentrations as low as 1 μM; instead of occupying and replacing the heart tissue within 8 days, the MCF-7/6 cells grew around the heart fragments and left it intact, when treated with these compounds. At the anti-invasive concentration of 1 μM, the three compounds did not affect the growth of the MCF-7/6 cells, as shown in the sulforhodamine B assay. Aggregate formation on agar was not stimulated by any of the three anti-invasive compounds, making an effect on the E-cadherin/catenin complex improbable. This is an invasion suppressor that can be activated in MCF-7/6 cells by a number of other molecules. Our data indicate that some polyphenolic and heterocyclic compounds are anti-invasive without being cytotoxic for the cancer cells.