119656-72-3

Basic information

• Product Name: Benzeneacetic acid, a-hydroxy-, butyl ester, (R)-
• CAS NO: 119656-72-3
• Molecular Formula: C12H16O3
• Molecular Weight: 208.257
• Mol File: 119656-72-3.mol

Chemical Properties

• CAS DataBase Reference: Benzeneacetic acid, a-hydroxy-, butyl ester, (R)-(CAS DataBase Reference)
• NIST Chemistry Reference: Benzeneacetic acid, a-hydroxy-, butyl ester, (R)-(119656-72-3)
• EPA Substance Registry System: Benzeneacetic acid, a-hydroxy-, butyl ester, (R)-(119656-72-3)

Safety Data

• Hazardous Substances Data: 119656-72-3(Hazardous Substances Data)

Upstream product

• 14007-02-4 butyl mandelate 
• 5524-55-0 n-butyl 2-oxo-2-phenylacetate 
• 122-43-0 butyl phenylacetate 
• 4358-87-6 (RS)-methyl mandelate 
• 71-36-3 butan-1-ol 
• 611-71-2 (R)-Mandelic Acid 
• 119718-86-4 (RS)-butyl O-acetylmandelate 
• 108-05-4 vinyl acetate 

Downstream Products

• 164386-47-4 (4S,6S)-6-((R)-Butoxycarbonyl-phenyl-methoxy)-4-phenyl-5,6-dihydro-4H-pyran-2-carboxylic acid methyl ester 
• 164386-44-1 (R)-Phenyl-vinyloxy-acetic acid butyl ester 

Relevant articles and documents

Improved Lipase-Mediated Resolution of Mandelic Acid Esters by Multivariate Investigation of Experimental Factors

Lipase catalyzed stereoselective acylation of butyl mandelate was studied.The determining role of solvent and acylating agent was pointed out and a considerable inhibitory effect due to mandelic acid was observed by screening different lipases.Finally, the performance of the reaction was appreciably improved thank to a multivariate approach.

Exploiting Cofactor Versatility to Convert a FAD-Dependent Baeyer–Villiger Monooxygenase into a Ketoreductase

Cyclohexanone monooxygenases (CHMOs) show very high catalytic specificity for natural Baeyer–Villiger (BV) reactions and promiscuous reduction reactions have not been reported to date. Wild-type CHMO from Acinetobacter sp. NCIMB 9871 was found to possess an innate, promiscuous ability to reduce an aromatic α-keto ester, but with poor yield and stereoselectivity. Structure-guided, site-directed mutagenesis drastically improved the catalytic carbonyl-reduction activity (yield up to 99 %) and stereoselectivity (ee up to 99 %), thereby converting this CHMO into a ketoreductase, which can reduce a range of differently substituted aromatic α-keto esters. The improved, promiscuous reduction activity of the mutant enzyme in comparison to the wild-type enzyme results from a decrease in the distance between the carbonyl moiety of the substrate and the hydrogen atom on N5 of the reduced flavin adenine dinucleotide (FAD) cofactor, as confirmed using docking and molecular dynamics simulations.

Autoamplification-Enhanced Oxidative Kinetic Resolution of sec-Alcohols and Alkyl Mandelates, and its Kinetic Model

In this contribution, the new dynamic nonlinear effect in asymmetric catalysis is discussed, manifesting itself in the oxidative kinetic resolution (OKR) of racemic secondary benzylic alcohols and alkyl mandelates with H2O2 in the presence of chiral Mn-based catalyst, with the apparent selectivity factor (krel) of the resolution being nonconstant over the reaction course. Typically, the initial growth of krel is changed into decay at high conversions. In this contribution, we demonstrate the oxidative kinetic resolution of various substrates bearing sec-alcoholic moieties, with the krel varying in different manners with increasing substrate conversion. We also present the predictive kinetic model of OKR with participation of asymmetric autoamplification. The influence of substrate and catalyst structure, as well as solvents and additives, on the behavior of krel variation, is discussed.

Chiral cobalt-catalyzed enantioselective aerobic oxidation of α-hydroxy esters

A chiral cobalt-catalyzed enantioselective aerobic oxidative kinetic resolution of (±)-α-hydroxy esters, using molecular oxygen as a sole oxidant, is reported and a maximum of selectivity factor (s) 31.9 was achieved with >99% enantiomeric excess for unreacted α-hydroxy esters.

Enantioselective α-hydroxylation of 2-arylacetic acid derivatives and buspirone catalyzed by engineered cytochrome P450 BM-3

Here we report that an engineered microbial cytochrome P450 BM-3 (CYP102A subfamily) efficiently catalyzes the α-hydroxylation of phenylacetic acid esters. This P450 BM-3 variant also produces the authentic human metabolite of buspirone, R-6-hydroxybuspir

The role of conformational flexibility of enzymes in the discrimination between amino acid and ester substrates for the subtilisin-catalyzed reaction in organic solvents

To investigate how the conformational flexibility of subtilisin affects its ability to discriminate between enantiomeric amino acid and ester substrates for the subtilisin-catalyzed reaction in an organic solvent, the flexibility around the active site and the surface of subtilisin was estimated from the mobility of a spin label bound to subtilisin by ESR spectroscopy. Many studies on enzyme flexibility focus on the active site. Both the surface and active site flexibility play an important role in the enantioselectivity enhancement of the enzyme-catalyzed reaction. It was found, however, that the different behavior observed for the enantioselectivity between the amino acid and ester substrates could be correlated with the flexibility around the surface rather than the flexibility at the active site of subtilisin. In other words, for the ester substrates, the greater flexibility around the surface of subtilisin induced by a conformational change resulting from the presence of an additive such as DMSO is essential for the enantioselectivity enhancement. This model is also supported by the Michaelis-Menten kinetic parameters for each enantiomeric substrate. Our findings provide insight into the enantioselectivity enhancement for the resolution of enantiomers for enzyme-catalyzed reactions in organic solvents.