5-Methoxycarbonylmethyluridine

Base Information

• Chemical Name: 5-Methoxycarbonylmethyluridine
• CAS No.: 29428-50-0
• Molecular Formula: C12H16 N2 O8
• Molecular Weight: 316.268
• DSSTox Substance ID: DTXSID20183642
• Nikkaji Number: J1.462.827D
• Wikidata: Q27109316
• Metabolomics Workbench ID: 53773
• Mol file: 29428-50-0.mol

Synonyms:5-MCMU;5-methoxycarbonylmethyluridine

Chemical Property of 5-Methoxycarbonylmethyluridine

Chemical Property:

• Boiling Point: °Cat760mmHg
• PKA: 8.99±0.10(Predicted)
• Flash Point: °C
• PSA: 151.34000
• Density: 1.57g/cm³
• LogP: -2.72410
• Storage Temp.: Hygroscopic, -20°C Freezer, Under inert atmosphere
• Solubility.: DMSO (Slightly), Methanol (Slightly), Water (Slightly)
• XLogP3: -2.2
• Hydrogen Bond Donor Count: 4
• Hydrogen Bond Acceptor Count: 8
• Rotatable Bond Count: 5
• Exact Mass: 316.09066547
• Heavy Atom Count: 22
• Complexity: 519

Purity/Quality:

97% ^*data from raw suppliers

5-Methoxycarbonylmethyluridine ^*data from reagent suppliers

Safty Information:

• Pictogram(s):  
• Hazard Codes: 

MSDS Files:

SDS file from LookChem

Useful:

• Canonical SMILES: COC(=O)CC1=CN(C(=O)NC1=O)C2C(C(C(O2)CO)O)O
• Isomeric SMILES: COC(=O)CC1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)CO)O)O
• General Description: 5-Pyrimidineacetic acid, 1,2,3,4-tetrahydro-2,4-dioxo-1-beta-D-ribofuranosyl-, methyl ester (also known as 5-methoxycarbonylmethyluridine or mcm5U) is a modified nucleoside that serves as a substrate for the AlkB domain of mammalian ABH8. This enzyme hydroxylates mcm5U at the wobble position of tRNA, converting it into 5-(S)-methoxycarbonylhydroxymethyluridine ((S)-mchm5U), a reaction dependent on iron(II) and α-ketoglutarate (aKG) cofactors. This modification highlights the role of ABH8 in RNA regulation and expands the functional diversity of AlkB family proteins beyond demethylation.

Technology Process of 5-Methoxycarbonylmethyluridine

There total 21 articles about 5-Methoxycarbonylmethyluridine which guide to synthetic route it. The literature collected by LookChem mainly comes from the sharing of users and the free literature resources found by Internet computing technology. We keep the original model of the professional version of literature to make it easier and faster for users to retrieve and use. At the same time, we analyze and calculate the most feasible synthesis route with the highest yield for your reference as below:

synthetic route:

Reference yield: 84.0%

2',3'-O-isopropylideneuridine-5-acetic acid methyl ester (110920-79-1) → 5-<(methylcarboxy)methyl>uridine (29428-50-0)

Guidance literature:

With trifluoroacetic acid; In water; for 0.5h; Ambient temperature;

Reference yield: 75.0%

methanol (67-56-1) + 5-(carboxymethyl)uridine (20964-06-1) → 5-<(methylcarboxy)methyl>uridine (29428-50-0)

Guidance literature:

With sulfuric acid; for 24h; Heating;

DOI:10.1021/ja00257a044

Reference yield: 72.0%

N3-benzoyl-2',3',5'-O-triacetoxyuridine-5-malonic acid dimethyl ester (1261157-40-7) → 5-<(methylcarboxy)methyl>uridine (29428-50-0)

Guidance literature:

With sodium methylate; In methanol; at 50 ℃; for 16h;

DOI:10.1002/anie.201001242

upstream raw materials:

5-Hydroxy-uridin

methyl (triphenylphosphoranylidene)acetate

2',3'-O-isopropylidene-5-methoxycarbonylmethyl-5'-O-methoxymethyluridine

2',3'-O-isopropylideneuridine-5-acetic acid methyl ester

Downstream raw materials:

5-(carbamoylmethyl)uridine

5'-O-(4,4'-dimethoxytrityl)-5-carbomethoxymethyluridine

N₃-benzoyl-2',3',5'-O-triacetoxyuridine-5-malonic acid dimethyl ester

Refernces

The AlkB domain of mammalian ABH8 catalyzes hydroxylation of 5-methoxycarbonylmethyluridine at the wobble position of tRNA

10.1002/anie.201001242

The research focuses on the AlkB domain of the mammalian ABH8 protein, which is part of the AlkB family of nonheme iron/α-ketoglutarate (aKG)-dependent dioxygenases. The study aimed to investigate the biochemical activity of ABH8, particularly its role in RNA modification. The researchers hypothesized that ABH8 could modify tRNAs through a controlled methylation/demethylation process. Through a series of experiments, they discovered that the AlkB domain of ABH8 catalyzes the hydroxylation of 5-methoxycarbonylmethyluridine (mcm5U) at the wobble position of tRNA, converting it into 5-(S)-methoxycarbonylhydroxymethyluridine ((S)-mchm5U). This modification was found to be specific to ABH8 and required the presence of iron(II) and aKG cofactors. The chemicals used in the process included iron and aKG as cofactors, l-ascorbic acid, and EDTA for quenching the reaction. The conclusions of the study suggest that ABH8 may play a role in regulating RNA function and could have implications in cancer progression, as it was previously shown to affect cancer cells. The findings also expand the understanding of the AlkB family of proteins, which were previously known for their demethylation activities, to include modification functions on nucleic acids.