328-51-8

Usage

Uses

Used in Organic Synthesis:
2-Oxooctanoic acid is used as a key building block in organic synthesis for its versatile reactivity, allowing for the creation of a wide range of pharmaceuticals, agrochemicals, and other fine chemicals.
Used in Pharmaceutical Production:
In the pharmaceutical industry, 2-Oxooctanoic acid is utilized as a key intermediate in the synthesis of certain amino acids and peptides, contributing to the development of new therapeutic agents.
Used in Agrochemical Production:
Similarly, in the agrochemical sector, 2-Oxooctanoic acid serves as an essential intermediate, facilitating the synthesis of various agrochemicals that are vital for agricultural applications.
Used in Metabolic Research:
2-Oxooctanoic acid is also used in metabolic research as it has been investigated for its role in energy metabolism, potentially offering insights into the development of therapeutic agents for metabolic disorders.
Used in Therapeutic Development:
Due to its potential biological activities, 2-Oxooctanoic acid is being explored as a possible therapeutic agent for certain metabolic disorders, indicating its importance in the field of medical research and treatment development.

InChI:InChI=1/C8H14O3/c1-2-3-4-5-6-7(9)8(10)11/h2-6H2,1H3,(H,10,11)

Upstream product

• 617-73-2 2-hydroxy-octanoic acid 
• 77785-25-2 (Z)-2-Methoxymethoxy-oct-2-enoic acid ethyl ester 
• 77785-29-6 (Z)-2-Methoxymethoxy-oct-2-enoic acid isopropyl ester 
• 79576-48-0 2-Ethoxy-2-methylsulfanylmethoxy-octanoic acid ethyl ester 
• 80490-46-6 4-hexyl-4-hydroxy-3-phenylisoxazoline-5-one 
• 80490-33-1 4-hexyl-3-phenylisoxazoline-5-one 
• 111-66-0 oct-1-ene 
• 124-07-2 Octanoic acid 
• 644-90-6 2-aminooctanoic acid 
• 118067-03-1 2-benzoyloctanoic acid ethyl ester 
• 3761-92-0 n-hexylmagnesium bromide 
• 79576-56-0 2-Butoxy-2-methylsulfanylmethoxy-octanoic acid butyl ester 
• 79576-52-6 2-Isopropoxy-2-methylsulfanylmethoxy-octanoic acid isopropyl ester 
• 77785-33-2 (Z)-2-Methoxymethoxy-oct-2-enoic acid butyl ester 

Downstream Products

• 74589-65-4 Z-2-(2,2-dimethylcyclopropanecarboxamido)-2-octenoic acid 
• 85394-14-5 (+)-(Z)-2-(2,2-dimethylcyclopropanecarboxamido)-2-octenoic acid 
• 109-67-1 1-penten 
• 19071-34-2 2-hydroxyacrylic acid 
• 617-73-2 2-hydroxy-octanoic acid 
• 79-21-0 peracetic acid 
• 127-17-3 2-oxo-propionic acid 
• 106819-03-8 (R)-α-aminooctanoic acid 
• 116783-26-7 (S)-α-aminooctanoic acid 
• 138901-11-8 2,2-difluoro-N-<4-(1H-tetrazol-5-ylmethyl)phenyl>octanamide 
• 1329710-30-6 N-benzyl-N-methyl-1-phenylnon-1-yn-3-amine 
• 644-90-6 2-aminooctanoic acid 
• 73252-30-9 1-(p-tolyl)heptan-1-one 
• 1607433-29-3 3-heptanoyl-1-methyl-4-phenyl-1-azaspiro[4.5]deca-3,6,9-triene-2,8-dione 

Relevant academic research and scientific papers

g-C3N4/metal halide perovskite composites as photocatalysts for singlet oxygen generation processes for the preparation of various oxidized synthons

g-C3N4/metal halide perovskite composites were prepared and used for the first time as photocatalysts forin situ1O2generation to perform hetero Diels-Alder, ene and oxidation reactions with suitable dienes and alkenes. The standardized methodology was made applicable to a variety of olefinic substrates. The scope of the method is finely illustrated and the reactions afforded desymmetrized hydroxy-ketone derivatives, unsaturated ketones and epoxides. Some limitations were also observed, especially in the case of the alkene oxidations, and poor chemoselectivity was somewhere observed in this work which is the first application of MHP-based composites forin situ1O2generation. The experimental protocol can be used as a platform to further expand the knowledge and applicability of MHPs to organic reactions, since perovskites offer a rich variety of tuning strategies which may be explored to improve reaction yields and selectivities.

Studies on the L-2-hydroxy-acid oxidase 2 catalyzed metabolism of S-mandelic acid and its analogues

Mandelic acid (MA) is generally used as a biomarker of the exposure of styrene, which is classified as a class of hazardous environmental pollutants, and also used as an important chiral intermediate in pharmaceutical industry. The previous studies have found the excretion of phenylglyoxylic acid (PGA) in human and rat, a metabolite of MA, was mainly from S-MA rather than R-MA. The metabolic mechanism, however, is not clear. In order to explore the possible metabolic mechanism, the enzyme types involved in the stereoselectivity metabolism of MA were firstly studied, and then human and rat long-chain 2-hydroxy-acid oxidase 2 (HAO2) were recombinantly expressed to study the metabolic profiles of S-MA and its analogues. The results indicated that HAO2 might catalyze the stereoselectivity metabolism of S-MA in rats. Human HAO2 (hHAO2) and rat HAO2 (rHAO2) isozymes β1 and β2 were successfully cloned and expressed with high purity and good enzyme activities. The enzyme kinetic profiles of these enzymes were different for S-MA and analogues. The order of catalytic efficiency for hHAO2 and rHAO2, however, was reverse. It might be relevance to the difference in active amino acid residues and loop 4 in human and rat L-2-hydroxy acid oxidase isozyme B crystal structures.

Enantioselective biocatalytic formal α-amination of hexanoic acid to l-norleucine

A three-step one-pot biocatalytic cascade was designed for the enantioselective formal α-amination of hexanoic acid to l-norleucine. Regioselective hydroxylation by P450CLA peroxygenase to 2-hydroxyhexanoic acid was followed by oxidation to the ketoacid by two stereocomplementary dehydrogenases. Combination with final stereoselective reductive amination by amino acid dehydrogenase furnished l-norleucine in >97% ee.

Biocatalytic Oxidative Cascade for the Conversion of Fatty Acids into α-Ketoacids via Internal H2O2 Recycling

The functionalization of bio-based chemicals is essential to allow valorization of natural carbon sources. An atom-efficient biocatalytic oxidative cascade was developed for the conversion of saturated fatty acids to α-ketoacids. Employment of P450 monooxygenase in the peroxygenase mode for regioselective α-hydroxylation of fatty acids combined with enantioselective oxidation by α-hydroxyacid oxidase(s) resulted in internal recycling of the oxidant H2O2, thus minimizing degradation of ketoacid product and maximizing biocatalyst lifetime. The O2-dependent cascade relies on catalytic amounts of H2O2 and releases water as sole by-product. Octanoic acid was converted under mild conditions in aqueous buffer to 2-oxooctanoic acid in a simultaneous one-pot two-step cascade in up to >99 % conversion without accumulation of hydroxyacid intermediate. Scale-up allowed isolation of final product in 91 % yield and the cascade was applied to fatty acids of various chain lengths (C6:0 to C10:0).

Enzymatic Resolution by a d-Lactate Oxidase Catalyzed Reaction for (S)-2-Hydroxycarboxylic Acids

Oxidase-catalyzed kinetic resolution is important for the production of enantiopure 2-hydroxycarboxylic acids (2-HAs), which are versatile building blocks for the synthesis of many significant compounds. However, in contrast to that of (R)-2-HAs, the production of (S)-2-HA is challenging because of the lack of related oxidases. Herein, suitable enzymes were screened systematically through the analysis of numerous putative d-lactate oxidase sequences and identification of several required properties. Finally, a d-lactate oxidase from Gluconobacter oxydans 621H with advantageous characteristics, such as good solubility, broad substrate spectrum, and high stereoselectivity, was selected to resolve 2-HAs into (S)-2-HAs. A variety of (S)-2-HAs was produced successfully using this d-lactate oxidase with excellent enantiomeric excess values (>99 %). The presented screening criteria and approach for target biocatalysis suggested a guideline for the production of optically active chemicals such as (S)-2-HAs.

Biocatalytic asymmetric synthesis of unnatural amino acids through the cascade transfer of amino groups from primary amines onto keto acids

Flee to the hills: An unfavorable equilibrium in the amino group transfer between amino acids and keto acids catalyzed by α-transaminases was successfully overcome by coupling with a ω-transaminase reaction as an equilibrium shifter, leading to efficient asymmetric synthesis of diverse unnatural amino acids, including L-tert-leucine and D-phenylglycine. Copyright

Method and product for skin lightening

A method and cosmetic product for lightening skin is provided, the method including wiping the skin with a cosmetic towelette. Impregnated on the towelette is an alpha-hydroxy carboxylic acid or salt thereof and a sunscreen agent.

Towelette product

A disposable towelette product is provided which includes a flexible water-insoluble substrate such as a tissue impregnated with an alpha- or beta-hydroxycarboxylic acid in a cosmetically acceptable carrier vehicle. Impregnated cosmetic composition in water will have a pH no higher than 6.8. A silicone microemulsion is present to minimize any stickiness resulting from deposition of the hydroxycarboxylic acid by the towelette onto the skin. In the presence of fatty acid group containing surfactants, the silicone microemulsion controls foul odors that the surfactants may emit through hydrolysis at low pH.

Towelette product for minimizing facial fine lines and wrinkles

A disposable towelette is provided which includes a flexible substrate such as a cellulosic tissue impregnated with an alpha-hydroxycarboxylic add delivered in a cosmetically acceptable carrier vehicle. There is further provided a method for cleansing skin and simultaneously inhibiting fine lines and wrinkles by wiping the skin with the impregnated towelette.

An Evaluation of the Substrate Specificity, and of Its Modification by Site-Directed Mutagenesis, of the Cloned L-Lactate Dehydrogenase from Bacillus stearothermophilus

The L-lactate dehydrogenase of Bacillus stearothermophilus (BSLDH) is a stable, thermophilic oxidoreductase.It has been selected as a model of enzymes with considerable future promise in assymetric synthesis in that it has been cloned to ensure a plentiful and inexpensive supply and because of the potential for tailoring its specificity to accept unnatural substrate structures via the site-directed mutagenesis techniques of moleculer biology.In this study, the specificity of BSLDH toward representative α-keto acids possessing straight- and branched-chain alkyl,cycloalkyl, or aromatic side chains has been evaluated.The results show that substrates that are sterically bulky in the region of the α-keto group to be reduced are poorly accepted by the enzyme.Graphics analyses indicated that the low activities of these hindered substrates might be partly due to a bad interaction of the active site residue Gln102 with large or branched substituents adjacent to the α-keto group.Accordingly, Gln102 has been replaced by the smaller Asn residue by site-directed mutagenesis in an attempt to expand the active site volume available to receive substrates larger than the natural pyruvate.However, the kinetic data show that bulky α-keto acids are only marginally better accommodated by the Gln102 -> Asn mutant than by the wild-type enzyme.