Disease relevance of C11348

• A remarkably increased enantioselectivity was obtained when the salt was added at 3-10 mol % versus substrate in the Burkholderia cepacia lipase (lipase PS-C)-catalyzed transesterification of 1-phenylethanol by using vinyl acetate in diisopropyl ether or a hexane solvent system [1].
• Acetylation of 1-phenylethanol catalyzed by lipase from Pseudomonas cepacia (PCL) was as fast and as enantioselective in ionic liquids as in toluene [2].
• Anaerobic mineralization of ethylbenzene by the denitrifying bacterium Azoarcus sp. strain EB1 was recently shown to be initiated by dehydrogenation of ethylbenzene to 1-phenylethanol [3].
• Escherichia coli cells transformed with tricistronic plasmids expressing these mutants readily gave 100-mg quantities of 4-hydroxydiphenylmethane and 1-phenylethanol in 24-72 h [4].

High impact information on C11348

• A solution containing mainly Delta/Lambda-c,c-3a reacts with acetophenone under Ar to give (S)-1-phenylethanol in 20% ee, whereas it is an active precatalyst for its hydrogenation under 5 atm H(2) to give 1-phenylethanol with an ee of 50-60% [5].
• Crystal structure and enzyme kinetics of the (S)-specific 1-phenylethanol dehydrogenase of the denitrifying bacterium strain EbN1 [6].
• Zeolite Beta with different Si/Al ratios was applied in the racemisation of (S)-1-phenylethanol [7].
• Both ethylbenzene dehydrogenase and 1-phenylethanol dehydrogenase activities were present in Azoarcus sp. strain EB1 cells that were grown anaerobically on ethylbenzene, 1-phenylethanol, and acetophenone, but these activities were absent in benzoate-grown cells [3].
• A distinct gene (ped) coding for (S)-1-phenylethanol dehydrogenase apparently forms an operon with the ebdABCD genes [8].

Chemical compound and disease context of C11348

• For the purpose of developing a new synthetic polymer containing an asymmetric molecule branch, three racemic alcohols, i.e. 1-phenylethanol, 1-(4-methylphenyl)ethanol and 1-(2-naphthyl)ethanol, were esterified enzymatically with divinyladipate using a lipase from Pseudomonas cepacia [9].

Biological context of C11348

• Specifically, in the lipase-catalyzed enantioselective acylation of racemic 1-phenylethanol, the (R)- and (S)-substrates are allowed to react separately in the wells of microtiter plates, the (R)-alcohol showing hot spots in the IR-thermographic images [10].

Anatomical context of C11348

• The enzyme kinetics of the initial hydroxylation of ethylbenzene to form 1-phenylethanol were determined in human liver microsomes [11].
• Production of 1-phenylethanol in hepatic microsomes exhibited biphasic kinetics with a high affinity, low Km, component (mean Km = 8 microM; V(max) = 689 pmol/min/mg protein; n = 6 livers) and a low affinity, high Km, component (Km = 391 microM; V(max) = 3039 pmol/min/mg protein; n = 6) [11].

Associations of C11348 with other chemical compounds

• Ethylbenzene was metabolized to 1-phenylethanol, acetophenone, 2-ethylphenol and 4-ethylphenol by rat liver microsomes [12].
• The products were found to be 1-phenylethanol and 1-phenylpropanol, respectively, by GC-MS and HPLC with a chiral column, with 100% enantiomeric excess of the (R-(+)-form [13].
• It was found out that, when used appropriately in combination with immobilized pea protein, immobilized ovalbumin made it possible to resolve and synthesize racemic 1-(2-naphthyl)ethanol, 1-phenylethanol, and 1-phenyl-1-propanol [14].

References