18997-57-4

Usage

Chemical Properties

White Powder

Uses

Different sources of media describe the Uses of 18997-57-4 differently. You can refer to the following data:
1. A fluorogenic substrate in the assay of ?-glucosidase. Fluorescence: max. Abs. 316nm; max. Em. 372nm; e x 10-3: 15
2. A fluorogenic substrate in the assay of ?-glucosidase.Fluorescence: max. Abs. 316nm; max. Em. 372nm; e x 10-3: 15
3. 4-Methylumbelliferyl β-D-glucopyranoside has been used as substrate:in glucosylceramidase β enzyme activity assay in lysosome-enriched fractions from primary hippocampal neuronsin β-glucosidase assay during yeast fermentationto assay glucocerebrosidase 1 (GBA1)-related glucosidase activity in macrophage cell line (RAW)

Definition

ChEBI: A beta-D-glucoside having a 4-methylumbelliferyl substituent at the anomeric position.

Biochem/physiol Actions

4-Methylumbelliferyl β-D-glucopyranoside is a synthetic enzymatic substrate for glycosidase. It has been used as substrate for the β- glucosidase from enterococci.

Purification Methods

4-Methylumbellifer-7-yl--Dglucopyranoside crystallises as the half hydrate from hot H2O. [Constantzas & Kocourek Collect Czech Chem Commun 24 1099 1959, De Re et al. Ann Chim (Rome) 4 9 2089 1959, Courtin-Duchateau & Veyrière Carbohydr Research 65 23, 29 1978, Beilstein 18 III/IV 5152, 8 IV 433, 18/7 V 616.]

Upstream product

• 67909-25-5 4′-methylumbelliferyl 2,3,4,6-tetra-O-acetyl-β-D-glucopyranoside 
• 618879-31-5 4-methylumbelliferyl β-laminaratetraoside 
• 618879-32-6 4-methylumbelliferyl β-laminarapentaoside 
• 90-33-5 7-hydroxy-4-methyl-chromen-2-one 
• 572-09-8 2,3,4,6-tetra-O-acetyl-α-D-glucopyranosyl bromide 
• 604-68-2 α-D-glucopyranose peracetylate 
• 133-89-1 UDP-glucose 
• 83-87-4 D-glucose pentaacetate 
• 3947-62-4 2,3,4,5-tetra-O-acetyl-D-glucopyranose 
• 74808-10-9 2,3,4,6-tetra-O-acetyl-d-glucopyranosyl trichloroacetimidate 
• 63700-19-6 uridine-5'-diphospho-α-D-glucuronic acid trisodium salt 
• 604-69-3 β-D-glucose pentaacetate 
• 572-09-8 2,3,4,6-tetra-O-acetyl-D-glucopyranosyl bromide 
• 4336-91-8 3-bromo-2-pyridyl 2,3,4,6-tetra-O-acetyl-β-D-glucopyranoside 

Downstream Products

• 6160-80-1 4-methylumbelliferyl-β-D-glucuronide 
• 90-33-5 7-hydroxy-4-methyl-chromen-2-one 
• 50-99-7 D-glucose 
• 2280-44-6 D-Glucose 
• 72626-61-0 4-methylumbellifer-7-yl-β-D-cellobioside 
• 172364-08-8 4-methylumbelliferyl 3-O-β-D-glucopyranosyl-β-D-glucopyranoside 
• 172364-16-8 4-methylumbelliferyl 2-O-benzyl-4,6-O-benzylidene-β-D-glucopyranoside 
• 172364-23-7 7-[(2S,3R,4S,5R,6R)-3-Benzyloxy-5-hydroxy-6-hydroxymethyl-4-((2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-2-yloxy]-4-methyl-chromen-2-one 
• 172364-19-1 4-methylumbelliferyl O-(2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl)-(1<*>3)-2-O-benzyl-4,6-benzylidene-β-D-glucopyranoside 
• 172364-20-4 4-methylumbelliferyl O-(2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl)-(1<*>4)-O-(2,3,6-tri-O-acetyl-β-D-glucopyranosyl)-(1<*>3)-2-O-benzyl-4,6-benzylidene-β-D-glucopyranoside 
• 73448-32-5 4-methylumbelliferyl β-D-galactopyranosyl-(1->4)-2-acetamido-2-deoxy-β-D-glucopyranoside 
• 937018-35-4 4-methylumbelliferyl-2,3,4-tri-O-acetyl-6-O-trityl-β-D-glucopyranoside 
• 492-61-5 β-D-glucose 
• 172364-12-4 4-methylumbelliferyl 4,6-O-benzylidene-β-D-glucopyranoside 

Relevant academic research and scientific papers

OleD Loki as a Catalyst for Tertiary Amine and Hydroxamate Glycosylation

We describe the ability of an engineered glycosyltransferase (OleD Loki) to catalyze the N-glycosylation of tertiary-amine-containing drugs and trichostatin hydroxamate glycosyl ester formation. As such, this study highlights the first bacterial model catalyst for tertiary-amine N-glycosylation and further expands the substrate scope and synthetic potential of engineered OleDs. In addition, this work could open the door to the discovery of similar capabilities among other permissive bacterial glycosyltransferases.

Glycyrrhetinic acid exhibits strong inhibitory effects towards UDP-glucuronosyltransferase (UGT) 1A3 and 2B7

The aim of the present study is to evaluate the inhibitory effects of liver UDP-glucuronosyltransferases (UGTs) by glycyrrhizic acid and glycyrrhetinic acid, which are the bioactive ingredients isolated from licorice. The results showed that glycyrrhetini

The Novel UDP Glycosyltransferase 3A2: Cloning, catalytic properties, and tissue distribution

The human UDP glycosyltransferase (UGT) 3A family is one of three families involved in the metabolism of small lipophilic compounds. Members of these families catalyze the addition of sugar residues to chemicals, which enhances their excretion from the body. The UGT1 and UGT2 family members primarily use UDP glucuronic acid to glucuronidate numerous compounds, such as steroids, bile acids, and therapeutic drugs. We showed recently that UGT3A1, the first member of the UGT3 family to be characterized, is unusual in using UDP N-acetylglucosamine as sugar donor, rather than UDP glucuronic acid or other UDP sugar nucleotides (J Biol Chem 283:36205-36210, 2008). Here, we report the cloning, expression, and characterization of UGT3A2, the second member of the UGT3 family. Like UGT3A1, UGT3A2 is inactive with UDP glucuronic acid as sugar donor. However, in contrast to UGT3A1, UGT3A2 uses both UDP glucose and UDP xylose but not UDP N-acetylglucosamine to glycosidate a broad range of substrates including 4-methylumbelliferone, 1-hydroxypyrene, bioflavones, and estrogens. It has low activity toward bile acids and androgens. UGT3A2 transcripts are found in the thymus, testis, and kidney but are barely detectable in the liver and gastrointestinal tract. The low expression of UGT3A2 in the latter, which are the main organs of drug metabolism, suggests that UGT3A2 has a more selective role in protecting the organs in which it is expressed against toxic insult rather than a more generalized role in drug metabolism. The broad substrate and novel UDP sugar specificity of UGT3A2 would be advantageous for such a function. Copyright

Molecular cloning and biochemical characterization of a new coumarin glycosyltransferase CtUGT1 from Cistanche tubulosa

UDP-glycosyltransferases (UGTs) are an important and functionally diverse family of enzymes involved in secondary metabolite biosynthesis. Coumarin is one of the most common skeletons of natural products with candidate pharmacological activities. However, to date, many reported GTs from plants mainly recognized flavonoids as sugar acceptors. Only limited GTs could catalyze the glycosylation of coumarins. In this study, a new UGT was cloned from Cistanche tubulosa, a valuable traditional tonic Chinese herb, which is abundant with diverse glycosides such as phenylethanoid glycosides, lignan glycosides, and iridoid glycosides. Sequence alignment and phylogenetic analysis showed that CtUGT1 is phylogenetically distant from most of the reported flavonoid UGTs and adjacent to phenylpropanoid UGTs. Extensive in vitro enzyme assays found that although CtUGT1 was not involved in the biosynthesis of bioactive glycosides in C. tubulosa, it could catalyze the glucosylation of coumarins umbelliferone 1, esculetine 2, and hymecromone 3 in considerable yield. The glycosylated products were identified by comparison with the reference standards or NMR spectroscopy, and the results indicated that CtUGT1 can regiospecifically catalyze the glucosylation of hydroxyl coumarins at the C7-OH position. The key residues that determined CtUGT1's activity were further discussed based on homology modeling and molecular docking analyses. Combined with site-directed mutagenesis results, it was found that H19 played an irreplaceable role as the crucial catalysis basis. CtUGT1 could be used in the enzymatic preparation of bioactive coumarin glycosides.

Solvent-Dependent Mechanism and Stereochemistry of Mitsunobu Glycosylation with Unprotected Pyranoses

An SN2 mechanism was proposed for highly stereoselective glycosylation of benzoic acid with unprotected α-d-glucose under Mitsunobu conditions in dioxane, while an SN1 mechanism was indicated for nonstereoselective glycosylation in DMF. The SN2-type stereoselective Mitsunobu glycosylation is generally applicable to various unprotected pyranoses as glycosyl donors in combination with a wide range of acidic glycosyl acceptors such as carboxylic acids, phenols, and imides, retaining its high stereoselectivity (33 examples). Glycosylation of a carboxylic acid with unprotected α-d-mannose proceeded also in an SN2 manner to directly afford a usually less accessible 1,2-cis-mannoside. One-or two-step total syntheses of five simple natural glycosides were performed using the glycosylation strategy presented here using unprotected α-d-glucose.

Based on 4 - methyl [...] synthesis method of a plurality of glycoside

The invention discloses a method for synthesizing various glucosides on a basis of 4-methylumbelliferone. According to the invention, a glycosyl donor peracetyl saccharide and a glycosyl acceptor 4-methylumbelliferone are subjected to a glycosylation reaction under room temperature or under heating with dichloromethane or 1,2-dichloroethane as a solvent and with the combined effect of Lewis acid boron trifluoride ethyl ether and organic alkali triethylamine or pyridine; and protecting groups are removed, such that various glucosides based on 4-methylumbelliferone can be obtained. The glucosides include 4-methylumbelliferone-beta-D-glucopyranosiduronide, 4-methylumbelliferone-beta-D-glucopyranoside, 4-methylumbelliferone-beta-D-xylopyranoside, 4-methylumbelliferone-beta-D-ribofuranoside, 4-methylumbelliferone-alpha-D-galactopyranoside, and 4-methylumbelliferone-alpha-D-mannopyranoside. The method is simple, and can produce a beta or alpha single-configuration target. A glycosylation reaction yield can reach 17-93%.

Glucosyltransferase Capable of Catalyzing the Last Step in Neoandrographolide Biosynthesis

ApUGT, a diterpene glycosyltransferase from Andrographis paniculata, could transfer a glucose to the C-19 hydroxyl moiety of andrograpanin to form neoandrographolide. This glycosyltransferase has a broad substrate scope, and it can glycosylate 26 natural and unnatural compounds of different structural types. This study provides a basis for exploring the glycosylation mechanism of ent-labdane-type diterpenes and plays an important role in diversifying the structures used in drug discovery.

Stereocontrolled Synthesis of Phenolic α-d-Glycopyranosides

Adopting the ‘remote activation concept’ toward stereocontrolled glycoside synthesis with minimal use of protection groups, a general synthesis of phenolic 1,2-cis glycopyranosides is reported, as exemplified by aryl α-d-galacto-, α-d-gluco- and 2-azido α-d-glucopyranosides among others using glycosyl donors bearing an anomeric (3-bromo-2-pyridyloxy) group and catalyzed by methyl triflate.

An improved helferich method for the α/β-stereoselective synthesis of 4-methylumbelliferyl glycosides for the detection of microorganisms

An improved Helferich method is presented. It involves the glycosylation of 4-methyl-umbelliferone with glycosyl acetates in the presence of boron trifluoride etherate combined with triethylamine, pyridine, or 4-dimethylaminopyridine under mild conditions, followed by deprotection to give fluorogenic 4-methylumbelliferyl glycoside substrates. Due to the use of base, the glycosylation reaction proceeds more easily, is uncommonly α- or β-stereoselective, and affords the corresponding products in moderate to excellent yields (51%-94%) under appropriate conditions.

Exploring the catalytic promiscuity of a new glycosyltransferase from Carthamus tinctorius

The catalytic promiscuity of a new glycosyltransferase (UGT73AE1) from Carthamus tinctorius was explored. UGT73AE1 showed the capability to glucosylate a total of 19 structurally diverse types of acceptors and to generate O-, S-, and N-glycosides, making it the first reported trifunctional plant glycosyltransferase. The catalytic reversibility and regioselectivity were observed and modeled in a one-pot reaction transferring a glucose moiety from icariin to emodin. These findings demonstrate the potential versatility of UGT73AE1 in the glycosylation of bioactive natural products.