43201-07-6

Basic information

• Product Name: Hexanoic acid, 2-hydroxy-, (2R)-
• Synonyms: Hexanoic acid, 2-hydroxy-, (2R)-
• CAS NO: 43201-07-6
• Molecular Formula: C₆H₁₂O₃
• Molecular Weight: 132
• Mol File: 43201-07-6.mol

Chemical Properties

• Melting Point: 62 °C
• Boiling Point: 270.0±0.0 °C(Predicted)
• Appearance: /
• Density: 1.100±0.06 g/cm3(Predicted)
• PKA: 3.86±0.21(Predicted)
• CAS DataBase Reference: Hexanoic acid, 2-hydroxy-, (2R)-(CAS DataBase Reference)
• NIST Chemistry Reference: Hexanoic acid, 2-hydroxy-, (2R)-(43201-07-6)
• EPA Substance Registry System: Hexanoic acid, 2-hydroxy-, (2R)-(43201-07-6)

Safety Data

• Hazardous Substances Data: 43201-07-6(Hazardous Substances Data)

Upstream product

• 52089-55-1 2-hydroxyhexanoic acid ethyl ester 
• 13022-85-0 2-oxo-hexanoic acid sodium salt 
• 108-05-4 vinyl acetate 
• 636-36-2 rac-2-hydroxyhexanoic acid 
• 142-62-1 hexanoic acid 
• 327-57-1 L-Norleucine 
• 64-17-5 ethanol 
• 542-69-8 1-iodo-butane 
• 327-56-0 D-norleucine 
• 91423-84-6 (2S)-2-bromohexanoic acid 
• 616-05-7 2-bromohexanoic acid 

Downstream Products

• 152830-08-5 (2R)-2-hydroxyhexanoic acid benzyl ester 
• 1201686-54-5 (5S)-N-[5-chloro-2-(1H-tetrazol-1-yl)benzyl]-1-[(2R)-2-hydroxyhexanoyl]-4,5-dihydro-1H-pyrazole-5-carboxamide 
• 1554345-53-7 (R)-benzyl 2-(2-hydroxyhexanamido)acetate 
• 152830-14-3 (2R)-2-(((3-phenylpropyl)hydroxyphosphoryl)oxy)hexanoic acid benzyl ester 
• 152830-22-3 (2R)-2-(((3-phenylpropyl)hydroxyphosphoryl)oxy)hexanoic acid 
• 1025947-65-2 (R)-5-Butyl-2-oxo-2-(3-phenyl-propyl)-2λ⁵-[1,3,2]dioxaphospholan-4-one 
• 442521-58-6 2-({2-[3-(tert-butyl-dimethyl-silanyloxy)-2-hydroxy-propyl]-4,5-dipentyl-phenyl}-methyl-amino)-hexanoic acid benzyl ester 
• 442525-53-3 2-({2-[3-(tert-butyl-dimethyl-silanyloxy)-2-hydroxy-propyl]-5-octyl-phenyl}-methyl-amino)-hexanoic acid benzyl ester 

Relevant articles and documents

Light-Driven Kinetic Resolution of α-Functionalized Carboxylic Acids Enabled by an Engineered Fatty Acid Photodecarboxylase

Chiral α-functionalized carboxylic acids are valuable precursors for a variety of medicines and natural products. Herein, we described an engineered fatty acid photodecarboxylase (CvFAP)-catalyzed kinetic resolution of α-amino acids and α-hydroxy acids, which provides the unreacted R-configured substrates with high yields and excellent stereoselectivity (ee up to 99 %). This efficient light-driven process requires neither NADPH recycling nor prior preparation of esters, which were required in previous biocatalytic approaches. The structure-guided engineering strategy is based on the scanning of large amino acids at hotspots to narrow the substrate binding tunnel. To the best of our knowledge, this is the first example of asymmetric catalysis by an engineered CvFAP.

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.

Glutathione-analogous peptidyl phosphorus esters as mechanism-based inhibitors of γ-glutamyl transpeptidase for probing cysteinyl-glycine binding site

γ-Glutamyl transpeptidase (GGT) catalyzing the cleavage of γ-glutamyl bond of glutathione and its S-conjugates is involved in a number of physiological and pathological processes through glutathione homeostasis Defining its Cys-Gly binding site is extremely important not only in defining the physiological function of GGT, but also in designing specific and effective inhibitors for pharmaceutical purposes Here we report the synthesis and evaluation of a series of glutathione-analogous peptidyl phosphorus esters as mechanism-based inhibitors of human and Escherichia coli GGTs to probe the structural and stereochemical preferences in the Cys-Gly binding site Both enzymes were inhibited strongly and irreversibly by the peptidyl phosphorus esters with a good leaving group (phenoxide) Human GGT was highly selective for l-aliphatic amino acid such as l-2-aminobutyrate (l-Cys mimic) at the Cys binding site, whereas E coli GGT significantly preferred l-Phe mimic at this site The C-terminal Gly and a l-amino acid analogue at the Cys binding site were necessary for inhibition, suggesting that human GGT was highly selective for glutathione (γ-Glu-l-Cys-Gly), whereas E coli GGT are not selective for glutathione, but still retained the dipeptide (l-AA-Gly) binding site The diastereoisomers with respect to the chiral phosphorus were separated Both GGTs were inactivated by only one of the stereoisomers with the same stereochemistry at phosphorus The strict recognition of phosphorus stereochemistry gave insights into the stereochemical course of the catalyzed reaction Ion-spray mass analysis of the inhibited E coli GGT confirmed the formation of a 1:1 covalent adduct with the catalytic subunit (small subunit) with concomitant loss of phenoxide, leaving the peptidyl moiety that presumably occupies the Cys-Gly binding site The peptidyl phosphonate inhibitors are highly useful as a ligand for X-ray structural analysis of GGT for defining hitherto unidentified Cys-Gly binding site to design specific inhibitors

Biocontrolled formal inversion or retention of L -α-amino acids to enantiopure (R)- or (S)-hydroxyacids

Natural L-α-amino acids and L-norleucine were transformed to the corresponding α-hydroxy acids by formal biocatalytic inversion or retention of absolute configuration. The one-pot transformation was achieved by a concurrent oxidation reduction cascade in aqueous media. A representative panel of enantiopure (R)- and (S)-2-hydroxy acids possessing aliphatic, aromatic and heteroaromatic moieties were isolated in high yield (67-85 %) and enantiopure form (>99 % ee) without requiring chromatographic purification.

Biocatalytic racemization of α-hydroxycarboxylic acids using a stereo-complementary pair of α-hydroxycarboxylic acid dehydrogenases

Biocatalytic racemization of aliphatic, (aryl)aliphatic and aromatic α-hydroxycarboxylic acids was achieved via a reversible oxidation-reduction sequence using a pair of stereo-complementary Prelog- and anti-Prelog d- and l-α-hydroxyisocaproate dehydrogenases from Lactobacillus confusus DSM 20196 and Lactobacillus paracasei DSM 20008, resp., overexpressed in Escherichia coli. The mild reaction conditions ensured essential 'clean' isomerization, undesired 'over-oxidation' of the substrate forming the α-ketoacid could be suppressed by exclusion of O2 and adjustment of the NAD+/NADH-ratio.

Biocatalytic racemization of aliphatic, arylaliphatic, and aromatic α-hydroxycarboxylic acids

Biocatalytic racemization of a range of aliphatic, (aryl)aliphatic, and aromatic α-hydroxycarboxylic acids was accomplished by using whole resting cells of a range of Lactobacillus spp. The mild (physiological) reaction conditions ensured an essentially "clean" isomerization in the absence of side reactions, such as elimination or decomposition. Whereas straight-chain aliphatic 2-hydroxy-carboxylic acids were racemized with excellent rates (up to 85% relative to lactate), steric hindrance was observed for branched-chain analogues. Good rates were observed for aryl-alkyl derivatives, such as 3-phenyllactic acid (up to 59%) and 4-phenyl-2-hydroxybutanoic acid (up to 47%). In addition, also mandelate and its o-chloro analogue were accepted at a fair rate (45%). This biocatalytic racemization represents an important tool for the deracemization of a number of pharmaceutically important building blocks.

Dynamic kinetic resolution via dual-function catalysis of modified cinchona alkaloids: Asymmetric synthesis of α-hydroxy carboxylic acids

A highly enantioselective catalytic transformation of racemic α-hydroxy acids to optically active α-hydroxy acids is reported. A new procedure was developed for the condensation of racemic α-hydroxy acids with trichloromethyl chloroformate (diphosgene) at room temperature in the presence of activated charcoal to form 5-substituted-1,3-dioxolane-2,4-diones in 90-100% yield. An efficient dynamic kinetic resolution of 5-aryl dioxolanediones was realized via a modified cinchona alkaloid-catalyzed alcoholytic opening of the dioxolanedione ring, generating a variety of optically active α-hydroxy esters in 91-96% ee and 61-85% chemical yield. In this dynamic kinetic resolution, the modified cinchona alkaloid was found to serve dual catalytic roles, mediating both the rapid racemization of the 5-aryl dioxolanediones and the enantioselective alcoholytic ring opening of the 5-aryl dioxolanediones. Consequently, both enantiomers of the 5-aryl dioxolanediones were converted to highly enantiomerically enriched aromatic α-hydroxy esters in yields (61-85%), far exceeding the maximum of 50% for a normal kinetic resolution. This development not only represents an expansion of the scope of asymmetric acyl-transfer catalysis of synthetic catalysts but also provides a new approach for the development of efficient chemical dynamic kinetic resolutions promoted by a single catalyst. 5-Alkyl dioxolanediones were resolved by a conventional but highly enantioselective kinetic resolution to provide α-hydroxy acids and esters in high optical purity and good yields. Copyright

Synthesis, conformation and PKC isozyme surrogate binding of new lactone analogues of benzolactam-V8s

To investigate the role of the amide hydrogen of benzolactam-V8s (1-3) on protein kinase C (PKC) isozyme binding, new lactone analogues of benzolactam-V8s with hydrophobic side chains at positions 8 and/or 9 (5-8) were synthesized. The PKC binding affinities of 8- and 9-decylbenzolactone-V8 (5,6) were much lower than those of 8- and 9-decylbenzolactam-V8 (2,3), respectively, indicating that the amide hydrogen of benzolactam-V8s plays a critical role in PKC binding. 8-Decylbenzolactam-V8 (2) showed lower binding affinities to all PKC isozymes compared with those of 9-decylbenzolactam-V8 (3). The binding affinities of 8-substituted benzolactones (5,7,8) were also lower than those of 9-decylbenzolactone-V8 (6), but their PKC isozyme selectivity was higher than those of 2, 3 and 6. 8-Decybenzolactone-V8 (5) exhibited the most significant η-C1B selectivity among the four benzolactones (5-8) synthesized in this study.

Cyclic AMP-specific phosphodiesterase inhibitors

Novel pyrrolidine compounds that are potent and selective inhibitors of PDE4, as well as methods of making the same, are disclosed. Use of the compounds in the treatment of inflammatory diseases and other diseases involving elevated levels of cytokines, as well as central nervous system (CNS) disorders, also is disclosed.

Quantitative transformation of racemic 2-hydroxy acids into (R)-2-hydroxy acids by enantioselective oxidation with glycolate oxidase and subsequent reduction of 2-keto acids with D-lactate dehydrogenase

The enzymatic resolution of chiral 2-hydroxy acids 1 by enantioselective oxidation with molecular oxygen in the presence of glycolate oxidase from spinach (Spinacia oleracea) and subsequent asymmetric reduction of 2-oxo acids 2 with D-lactate dehydrogenase from Lactobacillus leichmannii leads to enantiomerically pure (R)-2-hydroxy acids in up to 89% yield based on the racemate.