92367-54-9

Basic information

• Product Name: 3-(4-Hydroxy-butyl)-benzonitrile
• Synonyms: 3-(4-Hydroxy-butyl)-benzonitrile
• CAS NO: 92367-54-9
• Molecular Weight: 175.23
• Mol File: 92367-54-9.mol
• Article Data: 2

Chemical Properties

• CAS DataBase Reference: 3-(4-Hydroxy-butyl)-benzonitrile(CAS DataBase Reference)
• NIST Chemistry Reference: 3-(4-Hydroxy-butyl)-benzonitrile(92367-54-9)
• EPA Substance Registry System: 3-(4-Hydroxy-butyl)-benzonitrile(92367-54-9)

Safety Data

• Hazardous Substances Data: 92367-54-9(Hazardous Substances Data)

Upstream product

• 6952-59-6 3-cyanobromobenzene 
• 202208-79-5 3-(4-hydroxybut-1-yn-1-yl)benzonitrile 

Downstream Products

• 92422-91-8 4-(3-cyanophenyl)butanoic acid 
• 202208-86-4 Biphenyl-4-carboxylic acid {(E)-1-[2-(3-cyano-phenyl)-ethyl]-3-phenyl-allyl}-amide 
• 202208-82-0 2-[(Biphenyl-4-carbonyl)-amino]-4-(3-cyano-phenyl)-butyric acid methyl ester 
• 202208-83-1 2-[(Biphenyl-4-carbonyl)-amino]-4-(3-cyano-phenyl)-butyric acid 
• 202208-85-3 Biphenyl-4-carboxylic acid [3-(3-cyano-phenyl)-1-formyl-propyl]-amide 
• 202208-84-2 Biphenyl-4-carboxylic acid [3-(3-cyano-phenyl)-1-hydroxymethyl-propyl]-amide 
• 202208-81-9 2-Amino-4-(3-cyano-phenyl)-butyric acid methyl ester 
• 202208-80-8 4-(3-Cyano-phenyl)-butyric acid methyl ester 

Relevant articles and documents

Novel Propargyl-Linked Bisubstrate Analogues as Tight-Binding Inhibitors for Nicotinamide N-Methyltransferase

Nicotinamide N-methyltransferase (NNMT) catalyzes the methyl transfer from the cofactor S-adenosylmethionine to nicotinamide and other pyridine-containing compounds. NNMT is an important regulator for nicotinamide metabolism and methylation potential. Aberrant expression levels of NNMT have been implicated in cancer, metabolic, and neurodegenerative diseases, which makes NNMT a potential therapeutic target. Therefore, potent and selective NNMT inhibitors can serve as valuable tools to investigate the roles of NNMT in its mediated diseases. Here, we applied a rational strategy to design and synthesize the tight-binding bisubstrate inhibitor LL320 through a novel propargyl linker. LL320 demonstrates a Ki value of 1.6 ± 0.3 nM, which is the most potent inhibitor to date. The cocrystal structure of LL320 confirms its interaction with both the substrate and cofactor binding sites on NNMT. Importantly, this is the first example of using the propargyl linker to construct potent methyltransferase inhibitors, which will expand our understanding of the transition state of methyl transfer.