74133-20-3

Usage

Uses

Used in Pharmaceutical Industry:
4-Methoxypyridine-3-carbonitrile is utilized as an intermediate in the synthesis of various pharmaceuticals. Its unique structure allows it to be a key component in the development of new drugs, contributing to the advancement of medicinal chemistry.
Used in Agrochemical Industry:
In the agrochemical sector, 4-Methoxypyridine-3-carbonitrile serves as an intermediate for the production of agrochemicals. Its role in the synthesis of these compounds helps in the development of effective solutions for agricultural applications.
Used in Organic Compounds Synthesis:
4-Methoxypyridine-3-carbonitrile is employed as a building block in the production of heterocyclic compounds. Its versatile structure makes it a valuable component in the synthesis of a wide range of organic compounds, expanding the scope of organic chemistry.
Used in Research and Development:
4-Methoxypyridine-3-carbonitrile is also used in research and development settings to explore its potential applications and properties. Its unique characteristics make it an interesting subject for scientific investigation, potentially leading to new discoveries and applications in various fields.

InChI:InChI=1/C7H6N2O/c1-10-7-2-3-9-5-6(7)4-8/h2-3,5H,1H3

Upstream product

• 124-41-4 sodium methylate 
• 89284-61-7 4-chloro-nicotinonitrile 
• 82257-15-6 4-methoxynicotinaldehyde 
• 620-08-6 4-methoxypyridine 
• 95689-38-6 1,1-dicyano-4-(N,N-dimethylamino)-2-methoxy-1,3-butadiene 
• 33631-09-3 4-methoxypyridin-3-amine 
• 143-33-9 sodium cyanide 
• 98645-42-2 2-bromo-4-methoxypyridine-3-carbonitrile 
• 98645-43-3 2-chloro-3-cyano-4-methoxypyridine 

Downstream Products

• 609-70-1 4-hydroxynicotinic acid 
• 524-40-3 ricinin 

Relevant academic research and scientific papers

Characterization of nicotinamidases: Steady state kinetic parameters, classwide inhibition by nicotinaldehydes, and catalytic mechanism

Nicotinamidases are metabolic enzymes that hydrolyze nicotinamide to nicotinic acid. These enzymes are widely distributed across biology, with examples found encoded in the genomes of Mycobacteria, Archaea, Eubacteria, Protozoa, yeast, and invertebrates, but there are none found in mammals. Although recent structural work has improved our understanding of these enzymes, their catalytic mechanism is still not well understood. Recent data show that nicotinamidases are required for the growth and virulence of several pathogenic microbes. The enzymes of Saccharomyces cerevisiae, Drosophila melanogaster, and Caenorhabditis elegans regulate life span in their respective organisms, consistent with proposed roles in the regulation of NAD+ metabolism and organismal aging. In this work, the steady state kinetic parameters of nicotinamidase enzymes from C. elegans, Sa. cerevisiae, Streptococcus pneumoniae (a pathogen responsible for human pneumonia), Borrelia burgdorferi (the pathogen that causes Lyme disease), and Plasmodium falciparum (responsible for most human malaria) are reported. Nicotinamidases are generally efficient catalysts with steady state kcat values typically exceeding 1 s -1. The Km values for nicotinamide are low and in the range of 2 -110 μM. Nicotinaldehyde was determined to be a potent competitive inhibitor of these enzymes, binding in the low micromolar to low nanomolar range for all nicotinamidases tested. A variety of nicotinaldehyde derivatives were synthesized and evaluated as inhibitors in kinetic assays. Inhibitions are consistent with reaction of the universally conserved catalytic Cys on each enzyme with the aldehyde carbonyl carbon to form a thiohemiacetal complex that is stabilized by a conserved oxyanion hole. The S. pneumoniae nicotinamidase can catalyze exchange of 18O into the carboxy oxygens of nicotinic acid with H218O. The collected data, along with kinetic analysis of several mutants, allowed us to propose a catalytic mechanism that explains nicotinamidase and nicotinic acid 18O exchange chemistry for the S. pneumoniae enzyme involving key catalytic residues, a catalytic transition metal ion, and the intermediacy of a thioester intermediate.

SUBSTITUTED THIAZOLE DERIVATIVES BEARING 3-PYRIDYL GROUPS, PROCESS FOR PREPARING THE SAME AND USE THEREOF

The present invention provides a pharmaceutical composition having a steroid C17,20-lyase inhibitory activity, which is useful as a prophylactic or therapeutic agent of prostatism, tumor such as breast cancer and the like, more particularly, a steroid C17,20-lyase inhibitor containing a compound represented by the formula: wherein A1 is an aromatic hydrocarbon group optionally having substituents or a heterocyclic group optionally having substituents, one of A2 and A3 is a hydrogen atom, a halogen atom, a C1-4 aliphatic hydrocarbon group optionally having substituents or an optionally esterified carboxyl group, the other of A2 and A3 is an aromatic hydrocarbon group optionally having substituents or a heterocyclic group optionally having substituents, and at least one of A1, A2 and A3 is a 3-pyridyl group optionally having substituents, or a salt thereof or a prodrug thereof.