74879-33-7

Basic information

• Product Name: (S)-mandelic acid n-butyl ester
• Synonyms: (S)-mandelic acid n-butyl ester
• CAS NO: 74879-33-7
• Molecular Weight: 208.257
• Mol File: 74879-33-7.mol
• Article Data: 5

Chemical Properties

• CAS DataBase Reference: (S)-mandelic acid n-butyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-mandelic acid n-butyl ester(74879-33-7)
• EPA Substance Registry System: (S)-mandelic acid n-butyl ester(74879-33-7)

Safety Data

• Hazardous Substances Data: 74879-33-7(Hazardous Substances Data)

Upstream product

• 14007-02-4 butyl mandelate 
• 4358-87-6 (RS)-methyl mandelate 
• 71-36-3 butan-1-ol 
• 119718-86-4 (RS)-butyl O-acetylmandelate 
• 17199-29-0 (S)-Mandelic acid 
• 122-43-0 butyl phenylacetate 

Downstream Products

• 85805-89-6 (S)-butyl 2-acetoxy-2-phenylethanoate 
• 164386-45-2 (S)-(+)-2-vinyloxyphenylacetate de n-butyle 

Relevant articles and documents

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.

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.

Resolution of Secondary Alcohols Using Lipase in Diisopropyl Ether

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