19939-82-3

Usage

Uses

Used in Biochemical Research:
1-NAPHTHYL-BETA-D-GLUCOPYRANOSIDE is used as a substrate for the detection of β-glucosidase enzyme activity in various biological samples. Its hydrolysis by β-glucosidase results in the formation of 1-naphthol, a compound characterized by its yellow color and fluorescence, allowing for a convenient and sensitive measurement of enzyme activity.
Used in Enzyme Assay Development:
In the field of enzyme assay development, 1-NAPHTHYL-BETA-D-GLUCOPYRANOSIDE serves as a valuable tool for the creation of assays that can accurately measure the activity of β-glucosidase enzymes. Its ability to produce a detectable product upon enzymatic action makes it an ideal candidate for the development of assays that require high sensitivity and specificity.
Used in Pharmaceutical and Diagnostic Industries:
1-NAPHTHYL-BETA-D-GLUCOPYRANOSIDE is employed in the pharmaceutical and diagnostic industries for the assessment of β-glucosidase activity in drug discovery and development processes. Its use in these industries aids in the identification of potential enzyme inhibitors or activators, contributing to the advancement of therapeutic agents targeting β-glucosidase-related diseases.
Used in Academic Research:
In academic research, 1-NAPHTHYL-BETA-D-GLUCOPYRANOSIDE is utilized for studying the function and regulation of β-glucosidase enzymes. Its application in research settings facilitates a deeper understanding of the biological roles and mechanisms of these enzymes, which can lead to the discovery of novel therapeutic targets and strategies.

InChI:InChI=1/C16H18O6/c17-8-12-13(18)14(19)15(20)16(22-12)21-11-7-3-5-9-4-1-2-6-10(9)11/h1-7,12-20H,8H2/t12-,13?,14+,15?,16-/m0/s1

Upstream product

• 90-15-3 α-naphthol 
• 2492-87-7 4-nitrophenyl-β-D-glucoside 
• 133-89-1 UDP-glucose 
• 83-56-7 1,5-dihydroxynaphthalene 
• 14581-88-5 1-Naphthyl 2,3,4,6-tetra-O-acetyl-β-D-glucopyranoside 

Relevant academic research and scientific papers

Enzymatic glucosylation of unnatural naphthols by a promiscuous glycosyltransferase from Aloe arborescens

Enzymatic glucosylation of unnatural products by natural glycosyltransferases (GTs) has great potential in creating novel and bioactive glucosides. A new GT (AaGT3) from Aloe arborescens exhibited catalytic promiscuity and high efficiency to diverse unnatural naphthols. By combing the substrate flexibility and catalytic reversibility of AaGT3, a cost-effective enzymatic approach to novel and bioactive unnatural glucosides was established. These studies indicate the significant potential of promiscuous natural GTs in synthesis of unnatural bioactive glucosides in drug discovery.

Engineering faster transglycosidases and their acceptor specificity

Transglycosidases are enzymes that have the potential to catalyze the synthesis of a wide range of high-value compounds starting from biomass-derived feedstocks. Improving their activity and broadening the substrate range are important goals to enable the widespread application of this family of biocatalysts. In this work, we engineered 20 mutants of the rice transglycosidase Os9BGlu31 and evaluated their catalysis in 462 reactions over 18 different substrates. This allowed us to identify mutants that expanded their substrate range and showed high activity, including W243L and W243N. We also developed double mutants that show very high activity on certain substrates and exceptional specificity towards hydrolysis, such as L241D/W243N. In order to guide a more general use of Os9BGlu31 variants as transglycosylation catalysts, we built cheminformatics models based on topological descriptors of the substrates. These models showed useful predictive potential on the external validation set and are allowing the identification of efficient catalytic routes to novel phytohormone and antibiotic glucoconjugates of interest.