34298-85-6

Usage

Uses

Used in Pharmaceutical Applications:
4,5-dihydroxy-7-methyl-9,10-dioxo-9,10-dihydroanthracen-2-yl alpha-D-galactopyranoside is used as a potential bioactive compound for pharmaceutical applications due to its anthracen backbone, which has been studied for its anti-inflammatory, anticancer, and antiviral properties.
Used in Drug Delivery Systems:
4,5-dihydroxy-7-methyl-9,10-dioxo-9,10-dihydroanthracen-2-yl alpha-D-galactopyranoside is used as a potential drug delivery agent due to the presence of the sugar moiety, which can interact with biological systems and improve the compound's bioavailability and therapeutic outcomes.
Used in Research and Development:
4,5-dihydroxy-7-methyl-9,10-dioxo-9,10-dihydroanthracen-2-yl alpha-D-galactopyranoside is used as a research compound to further understand its full potential and applications in various industries, including pharmaceuticals, drug delivery, and other fields.

Upstream product

• 518-82-1 1,6,8-trihydroxy-3-methyl-9,10-anthraquinone 
• 572-09-8 2,3,4,6-tetra-O-acetyl-α-D-glucopyranosyl bromide 
• 133-89-1 UDP-glucose 
• 120221-14-9 (2-chloro-4-nitrophenyl)-β-D-glucopyranoside 

Relevant academic research and scientific papers

Two trifunctional leloir glycosyltransferases as biocatalysts for natural products glycodiversification

Two promiscuous Bacillus licheniformis glycosyltransferases, YdhE and YojK, exhibited prominent stereospecific but nonregiospecific glycosylation activity of 20 different classes of 59 structurally different natural and non-natural products. Both enzymes transferred various sugars at three nucleophilic groups (OH, NH2, SH) of diverse compounds to produce O-, N-, and S-glycosides. The enzymes also displayed a catalytic reversibility potential for a one-pot transglycosylation, thus bestowing a cost-effective application in biosynthesis of glycodiversified natural products in drug discovery.

On the Catalytic Activity of a GT1 Family Glycosyltransferase from Streptomyces venezuelae ISP5230

GT1 family glycosyltansferase, Sv0189, from Streptomyces venezuelae ISP5230 (ATCC 10721) was characterized. The recombinantly produced protein Sv0189 possessed UDP-glycosyltransferase activity. Screening, using an assay employing unnatural nitrophenyl glycosides as activated donors, resulted in the discovery of a broad substrate scope with respect to both acceptor molecules and donor sugars. In addition to polyphenols, including anthraquinones, simple aromatics containing primary or secondary alcohols, a variety of complex natural products and synthetic drugs were glucosylated or xylosylated by Sv0189. Regioselectivity was established through the isolation and characterization of glucosylated products. Sv0189 and homologous proteins are widely distributed among Streptomyces species, and their apparent substrate promiscuity reveals potential for their development as biocatalysts for glycodiversification.