142039-78-9

Basic information

• Product Name: 3-allylresorcinol
• Synonyms: 3-allylresorcinol
• CAS NO: 142039-78-9
• Molecular Weight: 150.177
• Mol File: 142039-78-9.mol
• Article Data: 4

Chemical Properties

• CAS DataBase Reference: 3-allylresorcinol(CAS DataBase Reference)
• NIST Chemistry Reference: 3-allylresorcinol(142039-78-9)
• EPA Substance Registry System: 3-allylresorcinol(142039-78-9)

Safety Data

• Hazardous Substances Data: 142039-78-9(Hazardous Substances Data)

Upstream product

• 20469-65-2 1-bromo-3,5-dimethoxybenzene 
• 89981-17-9 3,5-dimethoxy-1-phenylmagnesium chloride 
• 7051-16-3 1-chloro-3,5-dimethoxybenzene 
• 64118-89-4 Methoxyeugenol 

Downstream Products

• 500-49-2 5-propyl-1,3-benzenediol 

Relevant articles and documents

Structure–activity relationships and docking studies of hydroxychavicol and its analogs as xanthine oxidase inhibitors

Hydroxychavicol (HC), which is obtained from the leaves of Piper betle LINN. (Piperaceae), inhibits xanthine oxidase (XO) with an IC50 value of 16.7μM, making it more potent than the clinically used allopurinol (IC50=30.7μM). Herein, a structure–activity relationship analysis of the polar part analogs of HC was conducted and an inhibitor was discovered with a potency 13 times that of HC. Kinetic studies have revealed that HC and its active analog inhibit XO in an uncompetitive manner. The binding structure prediction of these inhibitor molecules to the XO complex with xanthine suggested that both compounds (HC and its analog) could simultaneously form hydrogen bonds with xanthine and XO.

Substrate selective catalysis by rhodium metallohosts

A novel supramolecular catalyst functioning according to the principles of enzymatic catalysis is described. It consists of a basket-shaped molecule to which a catalytically active Rh(I) complex is attached. The catalyst selectively hydrogenates and isomerizes allyl-substituted dihydroxyarene substrates that are bound in its cavity. The reactivity of this supramolecular catalyst and its affinity for several substrates is compared with that of the corresponding catalyst without a binding site. Features known from enzymatic catalysis, e.g. Michaelis-Menten kinetics and rate enhancement by cooperative binding, are described and discussed.