95310-87-5

Basic information

• Product Name: (S)-3-HYDROXYGLUTARATE ETHYL
• Synonyms: (S)-3-HYDROXYGLUTARATE ETHYL;ETHYL HYDROGEN-(S)-3-HYDROXYGLUTARATE
• CAS NO: 95310-87-5
• Molecular Formula: C₇H₁₂O₅
• Molecular Weight: 0
• Mol File: 95310-87-5.mol
• Article Data: 5

Chemical Properties

• Boiling Point: 363.8°C at 760 mmHg
• Flash Point: 150.5°C
• Appearance: /
• Density: 1.257g/cm³
• Vapor Pressure: 9.17E-07mmHg at 25°C
• Refractive Index: 1.473
• CAS DataBase Reference: (S)-3-HYDROXYGLUTARATE ETHYL(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-3-HYDROXYGLUTARATE ETHYL(95310-87-5)
• EPA Substance Registry System: (S)-3-HYDROXYGLUTARATE ETHYL(95310-87-5)

Safety Data

• Hazardous Substances Data: 95310-87-5(Hazardous Substances Data)

Usage

Description

(S)-3-Hydroxyglutarate ethyl, with the molecular formula C7H12O5, is a chemical compound that exists as a stereoisomer of 3-hydroxyglutaric acid. It is commonly found in certain fungi and bacteria and plays a crucial role in various biochemical pathways such as the Krebs cycle, fatty acid metabolism, and amino acid metabolism. (S)-3-HYDROXYGLUTARATE ETHYL also contributes to the regulation of gene expression and has been associated with diseases like cancer and neurodegenerative disorders.

Uses

Used in Pharmaceutical Industry:
(S)-3-Hydroxyglutarate ethyl is used as a research compound for its potential implications in disease mechanisms. It aids in understanding the role of this chemical in gene regulation and its association with various diseases, including cancer and neurodegenerative disorders.
Used in Biochemical Research:
(S)-3-Hydroxyglutarate ethyl is used as an inhibitor of the enzyme isocitrate dehydrogenase, which is involved in cellular metabolism and has been linked to cancer development. This application helps researchers study the effects of inhibiting this enzyme on cellular processes and its potential role in disease progression.
Used in Metabolic Studies:
As a part of the Krebs cycle, fatty acid metabolism, and amino acid metabolism, (S)-3-hydroxyglutarate ethyl is used to study the intricacies of these metabolic pathways and their regulation. This knowledge can be applied to develop therapeutic strategies for metabolic disorders and other related health issues.

InChI:InChI=1/C7H12O5/c1-2-12-7(11)4-5(8)3-6(9)10/h5,8H,2-4H2,1H3,(H,9,10)/t5-/m0/s1

Upstream product

• 32328-03-3 diethyl 3-hydroxyglutarate 

Downstream Products

• 1240466-86-7 benzyl 5-ethyl (R)-3-hydroxypentandioate 
• 128237-30-9 1-tert-butyl 5-ethyl 3-hydroxypentanedioate 
• 355806-00-7 rosuvastatin tert-butyl ester 
• 615556-98-4 tert-butyl (3R)-3-(tert-butyldimethylsilyloxy)-6-dimethoxyphosphinyl-5-oxohexanate 

Relevant articles and documents

Enantioselective hydrolysis of diethyl 3-hydroxyglutarate to ethyl (S)-3-hydroxyglutarate by immobilized Candida antarctica lipase B

Optically pure ethyl (S)-3-hydroxyglutarate [(S)-3-EHG] is used as a key precursor for synthesis of a variety of pharmaceutically important compounds. In this work, we established an efficient procedure for enantioselectively hydrolyzing diethyl 3-hydroxyglutarate (3-DHG) to optically active (S)-3-EHG employing immobilized Candida antarctica lipase B (Novozym 435). Under the optimized conditions: pH 7.0, agitation speed 200 rpm, temperature 40 °C, 3-DHG concentration 0.15 mol L-1, and enzyme loading 7 g L -1, (S)-3-EHG was prepared in above 95% ee value and 98.5% yield, and the reaction was free from external mass transfer and intra-particle diffusion limitations and kinetically controlled. The inhibitions of substrate (3-DHG) and product (3-EHG) were excluded because both displayed no decline in activity at elevated concentrations within the given ranges. In addition, ethanol, a byproduct of the reaction, inhibited lipase B following an uncompetitive inhibition pattern. The kinetic constants were obtained through non-linear regression, with values of Vmax 1.29 mmol min-1 g -1, Km 0.06 mol L-1, and Ki 0.37 mol L-1, respectively.

A chemoenzymatic approach to the stereocontrolled synthesis of the C1-C11 fragment of (+)-peloruside A

A highly efficient and diastereoselective synthesis of the C1C11 fragment of the marine natural product (+)-peloruside A has been developed. Through enzymatic desymmetrization of diethyl 3-hydroxyglutarate with lipase B from Candida antarctica a large-sca

Bifunctional chiral synthons via biochemical methods. 5. Preparation of (S)-ethyl hydrogen-3-hydroxyglutarate, key intermediate to (R)-4-amino-3-hydroxybutyric acid and L-carnitine

Microbial enantioselective hydrolysis of diethyl-3-hydroxyglutarate afforded (S)-ethyl hydrogen-3-hydroxyglutarate, which was transformed into (R)-4-amino-3-hydroxybutyric acid and L-carnitine, via a Curtius and Hunsdiecker rearrangement, respectively.