1143502-75-3

Usage

Uses

Used in Organic Synthesis:
5-Bromo-1,2-difluoro-3-methylbenzene is used as a building block in organic synthesis for the creation of a wide range of other chemicals. Its unique combination of bromine, fluorine, and methyl groups allows for the development of diverse chemical structures, making it a valuable component in the synthesis of complex organic molecules.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, 5-Bromo-1,2-difluoro-3-methylbenzene is utilized as a reagent for the production of pharmaceutical intermediates. Its presence in the synthesis process can contribute to the development of new drugs and medicines, enhancing the therapeutic potential of various pharmaceutical compounds.
Used in Agrochemical Production:
5-Bromo-1,2-difluoro-3-methylbenzene also finds application in the agrochemical sector, where it serves as a reagent in the synthesis of agrochemicals. Its role in this industry is crucial for the development of effective pesticides, herbicides, and other agricultural chemicals that protect crops and enhance agricultural productivity.

Upstream product

• 1143502-73-1 5-Bromo-2,3-difluoro-1-(iodomethyl)benzene 

Relevant academic research and scientific papers

Nonpolar nucleoside mimics as active substrates for human thymidine kinases

We describe the use of nonpolar nucleoside analogues of systematically varied size and shape to probe the mechanisms by which the two human thymidine kinases (TK1 and TK2) recognize and phosphorylate their substrate,thymidine. Comparison of polar thymidine with a nonpolar isostere, 2,4- difluorotoluene deoxyriboside, as substrates for the two enzymes establishes that TK1 requires electrostatic complementarity to recognize the thymine base with high efficiency. Conversely, TK2 does not and phosphorylates the hydrophobic shape mimic with efficiency nearly the same as the natural substrate. To test the response to nucleobase size, thymidine-like analogues were systematically varied by replacing the 2,4 substituents on toluene with hydrogen and the halogen series (H, F, Cl, Br, I). Both enzymes showed a distinct preference for substrates having the naturalsize. To examine the shape preference, we prepared four mono- and diflu orotoluene deoxyribosides with varying positions of substitutions. WhileTK1 did not accept these nonpolar analogues as substrates, TK2 did show varying levels of phosphorylation of the shape-varied set. This latter enzyme preferred toluene nucleoside analogues having steric projections at the 2 and 4 positions, as is found in thymine, and strongly disfavore d substitution at the 3-position. Steady-state kinetics measurements showed that the 4-fluoro compound (7) had an apparent Vmax/Kmax value within 14-fold of the natural substrate, and the 2,4-difluoro compound (1), which is the closest isostere of thymidine, had a value within 2.5-fold. The results establish that nucleoside recognition mechanisms for the two classes of enzymes are very different. On the basis of these data, nonpolar nucleosides are likely to be active in the nucleotide salvage pathway in human cells, suggesting new designs for future bioactive molecules.