97278-44-9

Usage

Uses

Used in Pharmaceutical Industry:
2-Pyridinecarboxylic acid, 6-(bromomethyl)-, ethyl ester is used as a building block for the production of various pharmaceuticals. Its unique structure and functional groups make it a valuable intermediate in the synthesis of drugs with potential therapeutic applications.
Used in Agrochemical Industry:
2-Pyridinecarboxylic acid, 6-(bromomethyl)-, ethyl ester is also used as a building block in the production of agrochemicals. Its versatility and reactivity can be harnessed to create new agrochemicals with improved properties and effectiveness.
Used in Specialty Chemicals Industry:
2-Pyridinecarboxylic acid, 6-(bromomethyl)-, ethyl ester is used in the synthesis of specialty chemicals, where its unique structure and functional groups can be utilized to create novel compounds with specific applications in various industries.
Used in Organic Synthesis:
As an intermediate in organic synthesis, 2-Pyridinecarboxylic acid, 6-(bromomethyl)-, ethyl ester can be employed in various chemical reactions and organic transformations to produce a wide range of compounds with different properties and applications.

Upstream product

• 128-08-5 N-Bromosuccinimide 
• 39640-51-2 ethyl 6-methylpyridine-2-carboxylate 
• 15658-60-3 diethyl-2,6-pyridinedicarbonyl ester 
• 41337-81-9 ethyl 6-(hydroxymethyl)pyridine-2-carboxylate 

Downstream Products

• 912934-68-0 C₁₅H₁₃Cl₂NO₂S 
• 890051-45-3 6-(4-iodo-phenoxymethyl)-pyridine-2-carboxylic acid ethyl ester 
• 863296-89-3 6-(2-cyanomethoxy-3-formyl-phenoxymethyl)-pyridine-2-carboxylic acid ethyl ester 

Relevant academic research and scientific papers

Aerobic C-H acetoxylation of 8-methylquinoline in PdII- pyridinecarboxylic acid systems: Some structure-reactivity relationships

Catalytic oxidative C-H acetoxylation of 8-methylquinoline as a model substrate with O2 as oxidant was performed using palladium(II) carboxylate catalysts derived from four different pyridinecarboxylic acids able to form palladium(II) chelates of different size. A comparison of the rates of the substrate C-H activation and the O2 activation steps shows that the C-H activation step is rate-limiting, whereas the O2 activation occurs at a much faster rate already at 20 C. The chelate ring size and the chelate ring strain of the catalytically active species are proposed to be the key factors affecting the rate of the C-H activation.

Development of metal-chelating inhibitors for the Class II fructose 1,6-bisphosphate (FBP) aldolase

It has long been suggested that the essential and ubiquitous enzyme fructose 1,6-bisphosphate (FBP) aldolase could be a good drug target against bacteria and fungi, since lower organisms possess a metal-dependant (Class II) FBP aldolase, as opposed to higher organisms which possess a Schiff-base forming (Class I) FBP aldolase. We have tested the capacity of derivatives of the metal-chelating compound dipicolinic acid (DPA), as well a thiol-containing compound, to inhibit purified recombinant Class II FBP aldolases from Mycobacterium tuberculosis, Pseudomonas aeruginosa, Bacillus cereus, Bacillus anthracis, and from the Rice Blast causative agent Magnaporthe grisea. The aldolase from M. tuberculosis was the most sensitive to the metal-chelating inhibitors, with an IC50 of 5.2 μM with 2,3- dimercaptopropanesulfonate (DMPS) and 28 μM with DPA. DMPS and the synthesized inhibitor 6-(phosphonomethyl)picolinic acid inhibited the enzyme in a time-dependent, competitive fashion, with second order rate constants of 273 and 270 M- 1 s- 1 respectively for the binding of these compounds to the M. tuberculosis aldolase's active site in the presence of the substrate FBP (KM 27.9 μM). The most potent first generation inhibitors were modeled into the active site of the M. tuberculosis aldolase structure, with results indicating that the metal chelators tested cannot bind the catalytic zinc in a bidentate fashion while it remains in its catalytic location, and that most enzyme-ligand interactions involve the phosphate binding pocket residues.

Inhibitors of 11-beta hydroxysteroid dehydrogenase type I

Novel compounds are provided which are 11-beta-hydroxysteroid dehydrogenase type I inhibitors. 11-beta-hydroxysteroid dehydrogenase type I inhibitors are useful in treating, preventing, or slowing the progression of diseases requiring 11-beta-hydroxysteroid dehydrogenase type I inhibitor therapy. These novel compounds have the structure: or stereoisomers or prodrugs or pharmaceutically acceptable salts thereof, wherein G, L, Q, Z, R6, R7, and R8 are defined herein.

Biaryloxymethylarenecarboxylic acids as glycogen synthase activators

The present invention relates to compounds of formula (I) wherein Ar, Ar2, R2, R3, R4, m, p and s are as defined in the description and claims, and pharmaceutically acceptable salts thereof. The compounds are useful for the treatment and/or prophylaxis of diseases that are associated with the activation of the glycogen synthase enzyme, such as diabetes.

SUBSTITUTED THIAZOLE AND PYRIMIDINE DERIVATIVES AS MELANOCORTIN RECEPTOR MODULATORS

The present invention provides substituted thiazole and pyrimidine derivatives of Formula (I), methods of their preparation, pharmaceutical compositions comprising the compounds of Formula (I), and methods of use in treating human or animal disorders. The compounds of the invention can be useful as inhibitors of action of AgRP on a melanocortin receptor and thus can be useful for the management, treatment, control, or the adjunct treatment of diseases which may be responsive to the modulation of melanocortin receptors including obesity-related disorders.