6635-22-9

Usage

Occurrence

Reported found in natural smoke flavors, uncured smoked pork, beer and wort.

InChI:InChI=1/C11H14O3/c1-4-5-8-6-9(13-2)11(12)10(7-8)14-3/h4-7,12H,1-3H3

Upstream product

• 6627-88-9 4-allyl-2,6-dimethoxyphenol 
• 1530-32-1 ethyltriphenylphosphonium bromide 
• 134-96-3 syringic aldehyde 
• 9005-53-2 lignin 
• 20675-96-1 Syringenin 
• 123-51-3 i-Amyl alcohol 
• 62-53-3 aniline 

Downstream Products

• 20395-20-4 Isovaleriansaeure-<2,6-dimethoxy-4-propenyl-phenylester> 
• 134-96-3 syringic aldehyde 

Relevant academic research and scientific papers

Bioinspired Selective Synthesis of Heterodimer 8-5′ or 8- O-4′ Neolignan Analogs

The bioinspired synthesis of heterodimer neolignan analogs is reported by single-electron oxidation of both alkenyl phenols and phenols individually, followed by a combination of the resultant radicals. This oxidative radical cross-coupling strategy can afford heterodimer 8-5′ or 8-O-4′ neolignan analogs selectively with the use of air as the terminal oxidant and copper acetate as the catalyst at room temperature.

Allyl/propenyl phenol synthases from the creosote bush and engineering production of specialty/commodity chemicals, eugenol/isoeugenol, in Escherichia coli

The creosote bush (Larrea tridentata) harbors members of the monolignol acyltransferase, allylphenol synthase, and propenylphenol synthase gene families, whose products together are able to catalyze distinct regiospecific conversions of various monolignols into their corresponding allyl- and propenyl-phenols, respectively. In this study, co-expression of a monolignol acyltransferase with either substrate versatile allylphenol or propenylphenol synthases in Escherichia coli established that various monolignol substrates were efficiently converted into their corresponding allyl/propenyl phenols, as well as providing proof of concept for efficacious conversion in a bacterial platform. This capability thus potentially provides an alternate source to these important plant phytochemicals, whether for flavor/fragrance and fine chemicals, or ultimately as commodities, e.g.; for renewable energy or other intermediate chemical purposes. Previous reports had indicated that specific and highly conserved amino acid residues 84 (Phe or Val) and 87 (Ile or Tyr) of two highly homologous allyl/propenyl phenol synthases (circa 96% identity) from a Clarkia species mainly dictate their distinct regiospecific catalyzed conversions to afford either allyl- or propenyl-phenols, respectively. However, several other allyl/propenyl phenol synthase homologs isolated by us have established that the two corresponding amino acid 84 and 87 residues are not, in fact, conserved.