89378-59-6

Basic information

• Product Name: Butanoic acid, 1-methylpropyl ester, (R)-
• CAS NO: 89378-59-6
• Molecular Formula: C8H16O2
• Molecular Weight: 144.214
• Mol File: 89378-59-6.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: Butanoic acid, 1-methylpropyl ester, (R)-(CAS DataBase Reference)
• NIST Chemistry Reference: Butanoic acid, 1-methylpropyl ester, (R)-(89378-59-6)
• EPA Substance Registry System: Butanoic acid, 1-methylpropyl ester, (R)-(89378-59-6)

Safety Data

• Hazardous Substances Data: 89378-59-6(Hazardous Substances Data)

Upstream product

• 819-97-6 sec-butyl butyrate 
• 123-20-6 vinyl n-butyrate 
• 78-92-2 iso-butanol 

Downstream Products

• 14898-79-4 (2R)-butan-2-ol 

Relevant articles and documents

Discovery and Redesign of a Family VIII Carboxylesterase with High (S)-Selectivity toward Chiral sec-Alcohols

Highly enantioselective lipase has been widely utilized in the preparation of versatile enantiopure chiral sec-alcohols through kinetic or dynamic kinetic resolution. Lipase is intrinsically (R)-selective, and it is difficult to obtain (S)-selective lipase. Recent crystal structures of a family VIII carboxylesterase have revealed that the spatial array of its catalytic triad is the mirror image of that of lipase but with a catalytic triad that is distinct from lipase. We, therefore, hypothesized that the family VIII carboxylesterase may exhibit (S)-enantioselectivity toward sec-alcohols similar to (S)-selective serine protease, whose catalytic triad is also spatially arrayed as its mirror image. In this study, a homologous enzyme (carboxylesterase from Proteobacteria bacterium SG_bin9, PBE) of a known family VIII carboxylesterase (pdb code: 4IVK) was prepared, which showed not only moderate (S)-selectivity toward sec-alcohols such as 3-butyn-2-ol and 1-phenylethyl alcohol but also (R)-selectivity toward particular sec-alcohols among the substrates explored. Furthermore, the (S)-selectivity of PBE has been significantly improved by rational redesign based on molecular modeling. Molecular modeling identified a binding pocket composed of Ser381, Ala383, and Arg408 for the methyl substituent of (R)-1-phenylethyl acetate and suggested that larger residues may increase the enantioselectivity by interfering with the binding of the slow-reacting enantiomer. As predicted, substituting Ser381with larger residues (Phe, Tyr, and Trp) significantly improved the (S)-selectivity of PBE toward all sec-alcohols explored, even the substrates toward which the wild-type PBE exhibits (R)-selectivity. For instance, the enantioselectivity toward 3-butyn-2-ol and 1-phenylethyl alcohol was improved from E = 5.5 and 36.1 to E = 2001 and 882, respectively, by single mutagenesis (S381F).

Mapping the substrate selectivity of novel lipase from pseudozyma hubeiensis SY62

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