unctions, glycosyltransferases are identified to be involved in a multitude of biological processes, such as cell ell communication, immune responses [4], cell signaling and epigenetic regulation of gene expression [7,8], and plant- and bacterial-cell wall biosynthesis [9,10]. As a corollary, the Bcl-2 Antagonist manufacturer disruption of those biological processes due to abnormal glycosyltransferase activity or expression can have a detrimental effect on thePublisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional CDK7 Inhibitor drug affiliations.Copyright: 2021 by the authors. Licensee MDPI, Basel, Switzerland. This short article is an open access short article distributed below the terms and situations on the Inventive Commons Attribution (CC BY) license ( creativecommons.org/licenses/by/ four.0/).Molecules 2021, 26, 6230. doi.org/10.3390/moleculesmdpi/journal/moleculesMolecules 2021, 26,2 ofcell, top to really serious illnesses, for instance cancer, inflammation, and diabetes [11,12]. Glycosyltransferase inhibitors are being developed for the remedy of those illnesses, at the same time as metabolic ailments, such as Morbus Gaucher, a lysosomal storage illness characterized by an accumulation of glucocerebrosides in several organs on account of dysfunctional downstream degradation machinery (glucocerebrosidase), causing detrimental neurological and muscular symptoms [13,14]. The first-line therapy for Gaucher is Glucocerebrosidase enzyme replacement therapy, that is a burdensome therapy because of the routine injections that the patients undertake. Glucosylceramide synthase (GCS) will be the GT that produces these glucocerebrosides making use of UDP-Glucose as a donor and ceramides as acceptor substrates. An option to the intense enzyme replacement therapy, the identification of a little molecule inhibitor of GCS that could lessen the glucosylceramide item within the brain and be administered orally, could possibly be a effective treatment of Gaucher disease (Substrate reduction therapy) [15]. Due to the significance of this class of enzymes, there is a have to have to develop bioassays to study their activity and their regulation or determine chemical compounds that modulate their activity. At the moment, measuring glycosyltransferase activity relies on classic strategies, for example the chromatographic separation of substrate and product or the detection of a radiolabeled product. When these assays have proved to become valuable when it comes to sensitivity and precision, they may be cumbersome as they demand washing steps and separation in the glycosylated solution for analysis and will not be simply configured for speedy screening [16]. Alternatively, many assay technologies not requiring the usage of radiochemicals had been created inside the final two decades [17]. Some of them are fluorescence-based assays that detect the nucleoside diphosphate making use of either fluorescent chemosensors [18,19] or fluorescent tracers combined with immunodetection [20]. These assays possess the benefit of getting universal for all GTs that release the detected nucleotide. However, specificity towards the nucleotide versus the nucleotide-sugar substrate can produce greater background; thus, decreasing the sensitivity and the accuracy with the assay. Additionally, chemosensors’ availability and synthesis cost could limit their widespread acceptance [17]. Other universal nucleotide detection assays relying on the enzyme-coupled generation of fluorescence or absorbance were also created for GT activity measurement [21,22]. The fluorescent GT assays rel
