80952-71-2

Usage

Uses

Used in Pharmaceutical Industry:
(R)-Ginsenoside Rh1 is used as an anti-cancer agent for its ability to inhibit the growth and proliferation of human breast cancer cells. It has demonstrated potential in targeting various signaling pathways and molecular targets associated with cancer progression, making it a promising candidate for cancer therapy.
Additionally, (R)-Ginsenoside Rh1 can be utilized in the development of novel drug delivery systems to enhance its bioavailability, efficacy, and targeted delivery to cancer cells, thereby improving treatment outcomes and reducing side effects.

InChI:InChI=1/C36H62O9/c1-19(2)10-9-13-36(8,43)20-11-15-34(6)26(20)21(38)16-24-33(5)14-12-25(39)32(3,4)30(33)22(17-35(24,34)7)44-31-29(42)28(41)27(40)23(18-37)45-31/h10,20-31,37-43H,9,11-18H2,1-8H3/t20?,21-,22+,23+,24?,25?,26?,27+,28-,29+,30?,31+,33+,34-,35+,36+/m0/s1

Upstream product

• 52286-58-5 ginsenoside Rf 
• 22427-39-0 ginsenoside-Rg₁ 
• 52286-59-6 ginsenoside Re 
• 1462261-07-9 C₆₉H₈₆O₁₄ 
• 133-89-1 UDP-glucose 
• 1453-93-6 20S-protopanaxatriol 
• 80418-25-3 20(S)-notoginsenoside R₂ 
• 22427-39-0 ginsenoside Rg₁ 

Downstream Products

• 98474-78-3 6α-O-β-D-glucopyranosyl-(20S,24R)-epoxydammarane-3β,12β,25-triol 
• 1453-93-6 20S-protopanaxatriol 

Relevant academic research and scientific papers

Glycoside Hydrolase Family 39 β-Xylosidases Exhibit β-1,2-Xylosidase Activity for Transformation of Notoginsenosides: A New EC Subsubclass

β-1,2-Xylosidase activity has not been recorded as an EC subsubclass. In this study, phylogenetic analysis and multiple sequence alignments revealed that characterized β-xylosidases of glycoside hydrolase family (GH) 39 were classified into the same subgroup with conserved amino acid residue positions participating in substrate recognition. Protein-ligand docking revealed that seven of these positions were probably essential to bind xylose-glucose, which is linked by a β-1,2-glycosidic bond. Amino acid residues in five of the seven positions are invariant, while those in two of the seven positions are variable with low frequency. Both the wild-type β-xylosidase rJB13GH39 and its mutants with mutation at the two positions exhibited β-1,2-xylosidase activity, as they hydrolyzed o-nitrophenyl-β-d-xylopyranoside and transformed notoginsenosides R1 and R2 to ginsenosides Rg1 and Rh1, respectively. The results suggest that all of these characterized GH 39 β-xylosidases probably show β-1,2-xylosidase activity, which should be assigned an EC number with these β-xylosidases as representatives.

Glycoside Hydrolase Family 39 β-Xylosidases Exhibit β-1,2-Xylosidase Activity for Transformation of Notoginsenosides: A New EC Subsubclass

β-1,2-Xylosidase activity has not been recorded as an EC subsubclass. In this study, phylogenetic analysis and multiple sequence alignments revealed that characterized β-xylosidases of glycoside hydrolase family (GH) 39 were classified into the same subgroup with conserved amino acid residue positions participating in substrate recognition. Protein-ligand docking revealed that seven of these positions were probably essential to bind xylose-glucose, which is linked by a β-1,2-glycosidic bond. Amino acid residues in five of the seven positions are invariant, while those in two of the seven positions are variable with low frequency. Both the wild-type β-xylosidase rJB13GH39 and its mutants with mutation at the two positions exhibited β-1,2-xylosidase activity, as they hydrolyzed o-nitrophenyl-β-d-xylopyranoside and transformed notoginsenosides R1 and R2 to ginsenosides Rg1 and Rh1, respectively. The results suggest that all of these characterized GH 39 β-xylosidases probably show β-1,2-xylosidase activity, which should be assigned an EC number with these β-xylosidases as representatives.

Use of a Promiscuous Glycosyltransferase from Bacillus subtilis 168 for the Enzymatic Synthesis of Novel Protopanaxatriol-Type Ginsenosides

Ginsenosides are the principal bioactive ingredients of Panax ginseng and possess diverse notable pharmacological activities. UDP-glycosyltransferase (UGT)-mediated glycosylation of the C6-OH and C20-OH of protopanaxatriol (PPT) is the prominent biological modification that contributes to the immense structural and functional diversity of PPT-type ginsenosides. In this study, the glycosylation of PPT and PPT-type ginsenosides was achieved using a promiscuous glycosyltransferase (Bs-YjiC) from Bacillus subtilis 168. PPT was selected as the probe for the in vitro glycodiversification of PPT-type ginsenosides using diverse UDP-sugars as sugar donors. Structural analysis of the newly biosynthesized products demonstrated that Bs-YjiC can transfer a glucosyl moiety to the free C3-OH, C6-OH, and C12-OH of PPT. Five PPT-type ginsenosides were biosynthesized, including ginsenoside Rh1 and four unnatural ginsenosides. The present study suggests flexible microbial UGTs play an important role in the enzymatic synthesis of novel ginsenosides.

Biotransformation of Ginsenosides Re and Rg1 into Rg2 and Rh1 by Thermostable β-Glucosidase from Thermotoga thermarum

The recombinant thermostable β-glucosidase from Thermotoga thermarum DSM 5069T exhibited high selectivity to catalyze the conversion of ginsenoside Re and Rg1 to the more pharmacologically active minor ginsenoside Rg2 and Rh1, respectively. At a concentration of 1.36 U/mL of the enzyme, a temperature of 85°C, and pH 5.5, 10 g/L ginsenoside Re was transformed into 8.02 g/L Rg2 within 60 min, and 2 g/L ginsenoside Rg1 was transformed into 1.56 g/L Rh1 within 60 min. This paper provides the first report on the production of ginsenoside Rg2 and Rh1 by a highly thermostable β-glucosidase.

Synthetic access toward the diverse ginsenosides

All the possible types of the protopanaxatriol and protopanaxadiol glycosides, the major active yet extremely heterogeneous principles of ginsengs, could be accessed by the present sequence of transformations, including global removal of the sugar residue

Isolation, synthesis and structures of ginsenoside derivatives and their anti-tumor bioactivity

Protopanaxatriol saponins obtained with AB-8 macroporous resin mainly consisted of ginsenosides Rgi and Re. A novel mono-ester of ginsenoside-Rh 1 (ginsenoside-ORh1) was synthesized through further enzymatic hydrolysis and octanoyl chloride modifications. A 53% yield was obtained by a facile synthetic method. The structures were identified on the basis of ID-NMR and 2D-NMR, as well as ESI-TOF-MS mass spectroscopic analyses. The isolated and synthetic compounds were applied in an anti-tumor bioassay, in which ginsenoside ORhi showed moderate effects on Murine H22 Hepatoma Cells.

Enzymatic preparation of ginsenosides Rg2, Rh1, and F1 from protopanaxatriol-type ginseng saponin mixture

During investigations on the hydrolysis of a protopanaxatriol-type saponin mixture by various glycoside hydrolases, it was found that two minor saponins, ginsenosides Rg2 and Rh1, were formed in high yields by crude β-galactosidase from Aspergillus oryzae and crude lactase from Penicillium sp., respectively. Moreover, a crude preparation of naringinase from Penicillium decumbens readily hydrolyzed a protopanaxatriol-type saponin mixture to give an intestinal bacterial metabolite, ginsenoside F1 as the main product. A crude preparation of hesperidinase from Penicillium sp. selectively hydrolyzed ginsenoside Re into ginsenoside Rg1. This is the first report on the enzymatic preparation of minor saponins, ginsenosides Rg2 and Rh1, and of an intestinal bacterial metabolite, ginsenoside F1, with a high efficiency from a protopanaxatriol-type saponin mixture.