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Hydroxywybutosine
Hydroxywybutosine is a crucial compound in the biomedical industry for treating viral infections, particularly those caused by the Herpes Simplex Virus (HSV). This antiviral drug inhibits the replication of HSV by targeting essential enzymes within infected cells. With its potent antiviral activity, Hydroxywybutosine proves to be a promising therapeutic option for managing viral infections, offering potential relief and improved patient outcomes.
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Catalog
BRP-02137
Synonyms
3H-Imidazo[1,2-a]purine-7-butanoic acid, 4,9-dihydro-β-hydroxy-α-[(methoxycarbonyl)amino]-4,6-dimethyl-9-oxo-3-β-D-ribofuranosyl-, methyl ester, (αS)-; Methyl (αS)-4,9-dihydro-β-hydroxy-α-[(methoxycarbonyl)amino]-4,6-dimethyl-9-oxo-3-β-D-ribofuranosyl-3H-imidazo[1,2-a]purine-7-butanoate; Methyl (2S)-4-(3-((2R,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl)-4,6-dimethyl-9-oxo-4,9-dihydro-3H-imidazo[1,2-a]purin-7-yl)-3-hydroxy-2-((methoxycarbonyl)amino)butanoate
CAS
945684-11-7
IUPAC Name
methyl (2S)-4-[3-[(2R,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]-4,6-dimethyl-9-oxoimidazo[1,2-a]purin-7-yl]-3-hydroxy-2-(methoxycarbonylamino)butanoate
Molecular Weight
524.49
Molecular Formula
C21H28N6O10
Canonical SMILES
CC1=C(N2C(=O)C3=C(N(C2=N1)C)N(C=N3)C4C(C(C(O4)CO)O)O)CC(C(C(=O)OC)NC(=O)OC)O
InChI
InChI=1S/C21H28N6O10/c1-8-9(5-10(29)12(19(33)35-3)24-21(34)36-4)27-17(32)13-16(25(2)20(27)23-8)22-7-26(13)18-15(31)14(30)11(6-28)37-18/h7,10-12,14-15,18,28-31H,5-6H2,1-4H3,(H,24,34)/t10?,11-,12?,14-,15-,18-/m1/s1
InChIKey
OBCAXUIWCCSJPT-JPZHCBQBSA-N
Density
1.75±0.1 g/cm3
Symbol
OHyW
Related CAS
84270-21-3 (Methyl 4,9-dihydro-β-hydroxy-α-[(methoxycarbonyl)amino]-4,6-dimethyl-9-oxo-1-β-D-ribofuranosyl-1H-imidazo[1,2-a]purine-7-butanoate)
Chemical Structure:
Reference Reading
1. Total synthesis of the hypermodified RNA bases wybutosine and hydroxywybutosine and their quantification together with other modified RNA bases in plant materials
Antje Hienzsch, Christian Deiml, Veronika Reiter, Thomas Carell. Chemistry. 2013 Mar 25;19(13):4244-8. doi: 10.1002/chem.201204209.
We report an efficient synthesis of the hypermodified natural tRNA modifications wybutosine (yW) and hydroxywybutosine (OHyW). We also describe the preparation of isotopically labeled analogues for precise quantification of yW and OHyW in different tissues including plant materials. The synthesis involved the formation of the unusual tricyclic ring structure of the bases by using a catalytic, intramolecular hydroamination reaction. The basis for the synthesis is also a stereoselective coupling reaction that allows the introduction of the fully substituted side chains to the tricyclic core structure. The isotopologues of yW and OHyW, together with other isotopically labeled tRNA modifications, were ultimately used in LC-MS quantification experiments to investigate the role of the modified bases in the translational process. Quantification was performed in the plant species Arabidopsis thaliana.
2. The nature of the modification at position 37 of tRNAPhe correlates with acquired taxol resistance
Yu Pan, Tong-Meng Yan, Jing-Rong Wang, Zhi-Hong Jiang. Nucleic Acids Res. 2021 Jan 11;49(1):38-52. doi: 10.1093/nar/gkaa1164.
Acquired drug resistance is a major obstacle in cancer therapy. Recent studies revealed that reprogramming of tRNA modifications modulates cancer survival in response to chemotherapy. However, dynamic changes in tRNA modification were not elucidated. In this study, comparative analysis of the human cancer cell lines and their taxol resistant strains based on tRNA mapping was performed by using UHPLC-MS/MS. It was observed for the first time in all three cell lines that 4-demethylwyosine (imG-14) substitutes for hydroxywybutosine (OHyW) due to tRNA-wybutosine synthesizing enzyme-2 (TYW2) downregulation and becomes the predominant modification at the 37th position of tRNAphe in the taxol-resistant strains. Further analysis indicated that the increase in imG-14 levels is caused by downregulation of TYW2. The time courses of the increase in imG-14 and downregulation of TYW2 are consistent with each other as well as consistent with the time course of the development of taxol-resistance. Knockdown of TYW2 in HeLa cells caused both an accumulation of imG-14 and reduction in taxol potency. Taken together, low expression of TYW2 enzyme promotes the cancer survival and resistance to taxol therapy, implying a novel mechanism for taxol resistance. Reduction of imG-14 deposition offers an underlying rationale to overcome taxol resistance in cancer chemotherapy.
3. Expanding role of the jumonji C domain as an RNA hydroxylase
Akiko Noma, Ryuichiro Ishitani, Megumi Kato, Asuteka Nagao, Osamu Nureki, Tsutomu Suzuki. J Biol Chem. 2010 Nov 5;285(45):34503-7. doi: 10.1074/jbc.M110.156398.
JmjC (Jumonji C) domain-containing proteins are known to be an extensive family of Fe(II)/2-oxoglutarate-dependent oxygenases involved in epigenetic regulation of gene expression by catalyzing oxidative demethylation of methylated histones. We report here that a human JmjC protein named Tyw5p (TYW5) unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxywybutosine, in tRNA(Phe) by catalyzing hydroxylation. The finding provides an insight into the expanding role of JmjC protein as an RNA hydroxylase.
