95614-85-0

Basic information

• Product Name: (S)-ETHYL 3-HYDROXY-4-METHYLPENTANOATE
• Synonyms: (S)-ETHYL 3-HYDROXY-4-METHYLPENTANOATE
• CAS NO: 95614-85-0
• Molecular Formula: C₈H₁₆O₃
• Molecular Weight: 160.21
• Mol File: 95614-85-0.mol

Chemical Properties

• Appearance: /
• CAS DataBase Reference: (S)-ETHYL 3-HYDROXY-4-METHYLPENTANOATE(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-ETHYL 3-HYDROXY-4-METHYLPENTANOATE(95614-85-0)
• EPA Substance Registry System: (S)-ETHYL 3-HYDROXY-4-METHYLPENTANOATE(95614-85-0)

Safety Data

• Hazardous Substances Data: 95614-85-0(Hazardous Substances Data)

Usage

Uses

Used in Flavor and Fragrance Industry:
(S)-ETHYL 3-HYDROXY-4-METHYLPENTANOATE is used as a flavoring agent for its distinctive fruity and sweet aroma, enhancing the sensory experience of various products in this industry.
Used in Pharmaceutical Industry:
(S)-ETHYL 3-HYDROXY-4-METHYLPENTANOATE serves as a precursor in the synthesis of pharmaceuticals, contributing to the development of new drugs and organic compounds for medical applications.
Used in Food Industry:
(S)-ETHYL 3-HYDROXY-4-METHYLPENTANOATE is used as a flavoring agent in the food industry, adding a pleasant taste to various food products and improving their overall appeal.
Used in Material Science and Bio-based Product Development:
(S)-ETHYL 3-HYDROXY-4-METHYLPENTANOATE has potential applications in the development of new materials and bio-based products, showcasing its versatility beyond the traditional industries it is known for.

Upstream product

• 7152-15-0 ethyl 4-methyl-3-oxo-pentanoate 
• 1006696-13-4 (S)-ethyl 4-methyl-3-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)pentanoate 
• 78-84-2 isobutyraldehyde 
• 623-48-3 ethyl iodoacetae 
• 141-52-6 sodium ethanolate 
• 64-17-5 ethanol 
• 93617-86-8 (4S)-(+)-3-bromoacetyl-4-(1-methylethyl)-2-oxazolidinone 
• 182417-51-2 ethyl (3R)-2,2-(ethylenedithio)-3-hydroxy-4-methylpentanoate 
• 95614-76-9 ethyl-(R)-(+)-(p-toluenesulfinyl)-N-methoxy-acetimidate 

Downstream Products

• 125873-95-2 (3S,5S)-(-)-2,6-dimethyl-3,5-heptanediol 
• 274905-39-4 (3R,4R,6S)-4-Hydroxy-6-isopropyl-3-methyl-tetrahydro-pyran-2-one 
• 274905-39-4 (3S,4S,6S)-4-Hydroxy-6-isopropyl-3-methyl-tetrahydro-pyran-2-one 

Relevant articles and documents

A highly efficient designer cell for enantioselective reduction of ketones

A designer cell, surf-crs-gdh, coexpressing carbonyl reductase (crs) and glucose dehydrogenase (gdh) on the cell surface has been constructed and its enzyme activities are compared with those of the corresponding cell, cyto-crs-gdh, coexpressing crs and gdh in cytosol. For various ketones, surf-crs-gdh exhibited 48- to 265-fold higher crs activity per unit protein compared to cyto-crs-gdh.

Asymmetric reformatsky reaction of aldehydes catalyzed by novel β -amino alcohols and zinc complexes

A series of β-amino alcohols derived from (1R, 2S)-2-amino-1,2- diphenylethanol and substituted salicylaldehydes as novel chiral tridentate ligands has been applied to an asymmetric Reformatsky reaction of aldehydes with ethyl iodoacetate in the presence

Highly enantioselective double reduction of phenylglyoxal to (R)-1-phenyl-1,2-ethanediol by one NADPH-dependent yeast carbonyl reductase with a broad substrate profile

The activity and enantioselectivity of a carbonyl reductase from Pichia pastoris GS115 were evaluated with a series of carbonyl compounds including aryl aldehydes, ketones, α- and β-ketoesters. This recombinant enzyme possessed a broad substrate profile with the ability of reducing both aldehydes and ketones. Especially, the enzyme catalyzed the double reduction of phenylglyoxal to (R)-1-phenyl-1,2-ethanediol with 99% yield and 99% ee by coupling with d-glucose dehydrogenase for the regeneration of cofactor NADPH, representing the first example of effective reduction of both aldehyde and ketone functional groups in one molecule by using only one enzyme. Furthermore, this study provides valuable information for guiding the future application of this versatile biocatalyst.

Chiral iridium catalysts bearing spiro pyridine-aminophosphine ligands enable highly efficient asymmetric hydrogenation of β-aryl β-ketoesters

Tons of TONs: Chiral iridium catalysts bearing ligand 1 are highly efficient for the asymmetric hydrogenation of β-substituted β-ketoesters. The product β-hydroxyesters are delivered in high yield with excellent enantioselectivities and high turnover numbers (TONs). cod= 1,5-cyclooctadiene.

Bisoxazolidine-catalyzed enantioselective reformatsky reaction

A readily available chiral bisoxazolidine catalyzes the asymmetric Reformatsky reaction between ethyl iodoacetate and aldehydes. In the presence of 10 mol % of the ligand, dimethylzinc, and air, this method produces ethyl 3-hydroxy-3-(4-aryl)propanoates in high yields and in 75 to 80% ee at room temperature within 1 h. In contrast to aromatic substrates, relatively low ee's are obtained with aliphatic aldehydes.

A chiral 6-membered n -heterocyclic carbene copper(I) complex that induces high stereoselectivity

A chiral 6-membered annulated N-heterocyclic (6-NHC) copper complex that catalyzes β-borylations with high yield and enantioselectivity was developed. The chiral 6-NHC copper complex is easy to prepare on the gram scale and is very active, showing 10000 turnovers at 0.01 mol % of catalyst without significant decrease of enantioselectivity and with useful reaction rates.

Catalytic asymmetric boration of acyclic α,β-unsaturated esters and nitriles

(Chemical Equation Presented) Asymmetrie β-boration of acyclic α,β-unsaturated carbonyl compounds provides ready access to enantioenriched functionalized organoboron compounds. A range of acyclic unsaturated esters and nitriles reacted with high enantioselectivity and good yields at room temperature using a copper catalyst and planar chiral diphosphine ligands (L).

Enzymatic ketone reduction: mapping the substrate profile of a short-chain alcohol dehydrogenase (YMR226c) from Saccharomyces cerevisiae

A short-chain alcohol dehydrogenase (YMR226c) from Saccharomyces cerevisiae was cloned and expressed in Escherichia coli, and the encoded protein was purified. The activity and enantioselectivity of this recombinant enzyme were evaluated with a series of ketones. The alcohol dehydrogenase (YMR226c) was found to effectively catalyze the enantioselective reductions of aryl-substituted acetophenones, α-chloroacetophenones, aliphatic ketones, and α- and β-ketoesters. While the enantioselectivity for the reduction of β-ketoesters was moderate, the acetophenone derivatives, aromatic α-ketoesters, some substituted α-chloroacetophenones, and aliphatic ketones were reduced to the corresponding chiral alcohols with excellent enantioselectivity. The enantiopreference of this enzyme generally followed Prelog's rule for the simple ketones. The ester functionality played some role in determining the enzyme's enantiopreference for the reduction of α- and β-ketoesters. The present study serves as a valuable guidance for the future applications of this versatile biocatalyst.

Stereoselective enzymatic synthesis of chiral alcohols with the use of a carbonyl reductase from Candida magnoliae with anti-prelog enantioselectivity

In our effort to search for carbonyl reductases with anti-Prelog enantioselectivity, the activity and enantioselectivity of a carbonyl reductase from Candida magnoliae have been examined with various ketones of diverse structures. This carbonyl reductase catalyzed the reduction of a series of ketones, α-and β-ketoesters, to anti-Prelog configurated alcohols in excellent optical purity. The usefulness of this carbonyl reductase has been demonstrated by synthesis of several chiral alcohol intermediates of pharmaceutical importance.

A recombinant ketoreductase tool-box. Assessing the substrate selectivity and stereoselectivity toward the reduction of β-ketoesters

The substrate selectivity and stereoselectivity of a series of ketoreductases were evaluated toward the reduction of two sets of β-ketoesters. Both the structural variety at β-position and the substituent at α-position greatly affected the activity and stereoselectivity of these ketoreductases. For the first set of β-ketoesters, at least one ketoreductase was found that catalyzed the formation of either (d) or (l) enantiomer of β-hydroxyesters from each substrate with high optical purity, with the only exception of ethyl (d)-3-hydroxy-3-phenylpropionate. For the second set of β-ketoesters with α-substituents, the situation is more complex. More commonly, a ketoreductase was found that formed one of the four diastereomers in optically pure form, with only a few cases in which enzymes could be found that formed two or more of the diastereomers in high optical purity. The continued development of new, more diverse ketoreductases will create the capability to produce a wider range of single diastereomers of 2-substituted-3-hydroxy acids and their derivatives.