81801-15-2

Basic information

• Product Name: (R)-(E)-3-octen-2-ol
• Synonyms: (R)-(E)-3-octen-2-ol
• CAS NO: 81801-15-2
• Molecular Weight: 128.214
• Mol File: 81801-15-2.mol

Chemical Properties

• CAS DataBase Reference: (R)-(E)-3-octen-2-ol(CAS DataBase Reference)
• NIST Chemistry Reference: (R)-(E)-3-octen-2-ol(81801-15-2)
• EPA Substance Registry System: (R)-(E)-3-octen-2-ol(81801-15-2)

Safety Data

• Hazardous Substances Data: 81801-15-2(Hazardous Substances Data)

Upstream product

• 57648-55-2 (E)-oct-3-en-2-ol 

Downstream Products

• 853017-06-8 (S)-methyl 2-(benzylamino)-hexanoate 
• 167563-03-3 (R,E)-4-((oct-3-en-2-yloxy)methyl)benzene 

Relevant articles and documents

Biocatalytic Enantioselective Oxidation of Sec-Allylic Alcohols with Flavin-Dependent Oxidases

The oxidation of allylic alcohols is challenging to perform in a chemo- as well as stereo-selective fashion at the expense of molecular oxygen using conventional chemical protocols. Here, we report the identification of a library of flavin-dependent oxidases including variants of the berberine bridge enzyme (BBE) analogue from Arabidopsis thaliana (AtBBE15) and the 5-(hydroxymethyl)furfural oxidase (HMFO) and its variants (V465T, V465S, V465T/W466H and V367R/W466F) for the enantioselective oxidation of sec-allylic alcohols. While primary and benzylic alcohols as well as certain sugars are well known to be transformed by flavin-dependent oxidases, sec-allylic alcohols have not been studied yet except in a single report. The model substrates investigated were oxidized enantioselectively in a kinetic resolution with an E-value of up to >200. For instance HMFO V465S/T oxidized the (S)-enantiomer of (E)-oct-3-en-2-ol (1 a) and (E)-4-phenylbut-3-en-2-ol with E>200 giving the remaining (R)-alcohol with ee>99% at 50% conversion. The enantioselectivity could be decreased if required by medium engineering by the addition of cosolvents (e. g. dimethyl sulfoxide).

Esterification in non-aqueous media: Activity and selectivity of porcine pancreas carboxylesterase depending on the structure of the alcoholic substrate

Enzymatic esterification in n-hexane was carried out using various unsaturated and aromatic (R,S)-alcohols, dodecanoic acid and a crude pancreatic extract. A 'model' was developed describing reactivity and selectivity of the enzymatic catalysis. These parameters were found to depend on the structural features of the side chains at the reactive chiral center. In several homologous series of substrates reversal of configuration of the preferred enantiomer was observed. The evaluated 'model' will be a helpful tool to establish future synthetic strategies.