112100-39-7

Usage

Uses

Used in Food and Beverage Industry:
BUTANOIC ACID, 3-HYDROXY-4-IODO-, ETHYL ESTER, (S) is used as a flavoring agent to impart a pleasant taste and aroma to food and beverages.
Used in Perfumery:
BUTANOIC ACID, 3-HYDROXY-4-IODO-, ETHYL ESTER, (S) is used as a fragrance component in the production of perfumes, enhancing their scent profile.
Used in Personal Care Products:
BUTANOIC ACID, 3-HYDROXY-4-IODO-, ETHYL ESTER, (S) is used as a scenting agent in personal care products such as soaps, lotions, and shampoos, providing a pleasant and attractive fragrance.
Used in Pharmaceutical Industry:
BUTANOIC ACID, 3-HYDROXY-4-IODO-, ETHYL ESTER, (S) is used as a building block for the synthesis of various pharmaceutical compounds, contributing to the development of new drugs and medications.

InChI:InChI=1/C6H11IO3/c1-2-10-6(9)3-5(8)4-7/h5,8H,2-4H2,1H3/t5-/m1/s1

Upstream product

• 638-07-3 ethyl (2-chloroaceto)acetate 
• 81302-78-5 ethyl 4-iodo-3-oxobutanoate 
• 10488-69-4 ethyl (S)-4-chloro-3-hydroxybutanoate 
• 16029-98-4 trimethylsilyl iodide 
• 5469-16-9 (3S)-hydroxy-γ-butyrolactone 
• 64-17-5 ethanol 

Downstream Products

• 118856-11-4 (R)-(-)-Ethyl 3-hydroxy-4-phenylbutanoate 
• 2305-25-1 ethyl (R)-3-hydroxyhexanoate 
• 151763-75-6 (R)-3-hydroxytetradecanoic acid ethyl ester 
• 141942-85-0 (R)-ethyl 4-cyano-3-hydroxybutyrate 
• 112083-63-3 ethyl (-)-(2S)-oxirane-2-acetate 

Relevant academic research and scientific papers

Straightforward and efficient synthesis of (4R,6S)-4-(tert-butyldimethyl- siloxy)-6-(hydroxymethyl)tetrahydropyran-2-one

A novel synthetic approach to (4R,6S)-4-(tert-butyldimethylsiloxy)-6- (hydroxymethyl)tetrahydropyran-2-one, a key precursor of statin side chain, is described. A prime feature of the presented strategy is the transformation of (4R,6S)-4-(tert-butyldimethylsiloxy)-6-(iodomethyl)tetrahydropyran-2-one to an acetate ester derivative and subsequent cleavage of an acetate protection by applying homogeneous tin catalysis. Iodolactone used in the study is accessible by a new route in five steps from (S)-ethyl 4-chloro-3-hydroxybutanoate. This method overcomes many of the drawbacks associated with previously reported approaches. It gives the title compound in 21% over seven steps, which is the highest attained overall yield yet. The disclosed approach was realized in convenient and economical manner suitable for industrial use.

A Concise Stereoselective Total Synthesis of Methoxyl Citreochlorols and Their Structural Revisions

A concise, stereoselective and protecting group free approaches for the total synthesis of (?)-(2S,4R)- and (+)-(2R,4S)-3′-methoxyl citreochlorols and their stereoisomers are demonstrated. All four stereoisomers were synthesized to establish the absolute stereochemistry of the reported structures and the structures were revised accordingly. The approach involves chelation controlled regioselective reduction of a diester, silyl iodide promoted ring-opening iodo esterification of lactones, highly chemo- and regioselective ring-opening of an epoxy ester, dichloromethylation of a carboxyl group, and syn- and anti-selective reduction of the resulted β-hydroxy ketone as key steps.

SUBSTITUTED STRAIGHT CHAIN SPIRO DERIVATIVES

Provided herein are pharmaceutical agents useful for therapy and/or prophylaxis in a mammal, pharmaceutical composition comprising such compounds, and their use as menin/MLL protein/protein interaction inhibitors, useful for treating diseases such as cancer, including but not limited to leukemia, myelodysplastic syndrome (MDS), and myeloproliferative neoplasms (MPN); and diabetes.

Cation-π interactions contribute to substrate recognition in γ-butyrobetaine hydroxylase catalysis

γ-Butyrobetaine hydroxylase (BBOX) is a non-heme FeII- and 2-oxoglutarate-dependent oxygenase that catalyzes the stereoselective hydroxylation of an unactivated C-H bond of γ-butyrobetaine (γBB) in the final step of carnitine biosynthesis. BBOX contains an aromatic cage for the recognition of the positively charged trimethylammonium group of the γBB substrate. Enzyme binding and kinetic analyses on substrate analogues with P and As substituting for N in the trimethylammonium group show that the analogues are good BBOX substrates, which follow the efficiency trend N+>P+>As+. The results reveal that an uncharged carbon analogue of γBB is not a BBOX substrate, thus highlighting the importance of the energetically favorable cation-π interactions in productive substrate recognition. What's in the BBOX? Enzyme kinetics and substrate binding studies reveal that γ-butyrobetaine hydroxylase (BBOX)-catalyzed stereoselective hydroxylation of γ-butyrobetaine involves energetically favorable cation-π interactions.

Study of Class i and Class III Polyhydroxyalkanoate (PHA) Synthases with Substrates Containing a Modified Side Chain

Polyhydroxyalkanoates (PHAs) are carbon and energy storage polymers produced by a variety of microbial organisms under nutrient-limited conditions. They have been considered as an environmentally friendly alternative to oil-based plastics due to their renewability, versatility, and biodegradability. PHA synthase (PhaC) plays a central role in PHA biosynthesis, in which its activity and substrate specificity are major factors in determining the productivity and properties of the produced polymers. However, the effects of modifying the substrate side chain are not well understood because of the difficulty to accessing the desired analogues. In this report, a series of 3-(R)-hydroxyacyl coenzyme A (HACoA) analogues were synthesized and tested with class I synthases from Chromobacterium sp. USM2 (PhaCCs and A479S-PhaCCs) and Caulobacter crescentus (PhaCCc) as well as class III synthase from Allochromatium vinosum (PhaECAv). It was found that, while different PHA synthases displayed distinct preference with regard to the length of the alkyl side chains, they could withstand moderate side chain modifications such as terminal unsaturated bonds and the azide group. Specifically, the specific activity of PhaCCs toward propynyl analogue (HHxyCoA) was only 5-fold less than that toward the classical substrate HBCoA. The catalytic efficiency (kcat/Km) of PhaECAv toward azide analogue (HABCoA) was determined to be 2.86 × 105 M-1 s-1, which was 6.2% of the value of HBCoA (4.62 × 106 M-1 s-1) measured in the presence of bovine serum albumin (BSA). These side chain modifications may be employed to introduce new material functions to PHAs as well as to study PHA biogenesis via click-chemistry, in which the latter remains unknown and is important for metabolic engineering to produce PHAs economically.

Diacyltransferase Activity and Chain Length Specificity of Mycobacterium tuberculosis PapA5 in the Synthesis of Alkyl β-Diol Lipids

Although they are classified as Gram-positive bacteria, Corynebacterineae possess an asymmetric outer membrane that imparts structural and thereby physiological similarity to more distantly related Gram-negative bacteria. Like lipopolysaccharide in Gram-negative bacteria, lipids in the outer membrane of Corynebacterineae have been associated with the virulence of pathogenic species such as Mycobacterium tuberculosis (Mtb). For example, Mtb strains that lack long, branched-chain alkyl esters known as dimycocerosates (DIMs) are significantly attenuated in model infections. The resultant interest in the biosynthetic pathway of these unusual virulence factors has led to the elucidation of many of the steps leading to the final esterification of the alkyl β-diol, phthiocerol, with branched-chain fatty acids known as mycocerosates. PapA5 is an acyltransferase implicated in these final reactions. Here, we show that PapA5 is indeed the terminal enzyme in DIM biosynthesis by demonstrating its dual esterification activity and chain-length preference using synthetic alkyl β-diol substrate analogues. By applying these analogues to a series of PapA5 mutants, we also revise a model for the substrate binding within PapA5. Finally, we demonstrate that the Mtb Ser/Thr kinases PknB and PknE modify PapA5 on three overlapping Thr residues and that a fourth Thr is unique to PknE phosphorylation. These results clarify the DIM biosynthetic pathway and indicate post-translational modifications that warrant further elucidation for their roles in the regulation of DIM biosynthesis.

SYNTHETIC DERIVATIVES OF MPL AND USES THEREOF

In one aspect, the present disclosure provides compounds of formulae (I) and (II). In another aspect, a compound of formula (I) or (II) is formulated into compositions with an antigen, optionally with a vesicle. In some embodiments, compositions are administered intramuscularly.

Calorimetric insight into coupling between functionalized primary alkyl halide and vinylic organocuprate reagent: experimental determination of reaction enthalpies in the synthesis of (R)-ethyl 3-(tert-butyldimethylsilyloxy) hex-5-enoate- A key lactonized statin side chain precursor

The first calorimetric study of coupling between organocuprate, derived from Grignard reagent (vinyl magnesium chloride), and primary alkyl halide (e.g. (S)-ethyl 3-(tert-butyldimethylsilyloxy)-4-iodobutanoate) has been conducted. This transformation is paramountly important for efficient preparation of (R)-ethyl 3-(tert-butyldimethylsilyloxy)hex-5- enoate - a key lactonized statin side chain precursor. The results obtained give thorough calorimetric insight into this complex low-temperature synthesis as well as a new understanding of the suggested reductive elimination of the final intermediates in the coupling reaction. Namely, the surprising unexpected spontaneous three-step exothermal event has been observed during controlled progressive heating of the mixture of the final intermediates to the room temperature. This phenomenon confirms that coupling between functionalized primary alkyl halide and vinylic organocuprate reagent is not a simple SN2 substitution reaction. The presented study provides among others the first reported values of reaction enthalpies and corresponding adiabatic temperature rises of reaction mixture for all exothermic events that occurred in the (R)-ethyl 3-(tert-butyldimethylsilyloxy) hex-5-enoate synthesis. The obtained results ensure consequential thermal process safety knowledge which can be incorporated into safe process scale-up as well as design of reactor system with sufficient cooling capacity for industrial production of (R)-ethyl 3-(tert-butyldimethylsilyloxy)hex-5-enoate. Moreover, the results provide a basic guidance for other organocuprate coupling reaction systems.

Process for the synthesis of HMG-CoA reductase inhibitors

A novel synthesis of statins uses Wittig reaction of a heterocyclic core of statin with a lactonized side chain already possessing needed stereochemistry. Any separation of diastereoisomers is preformed early in the course of synthesis.

Towards EPC-syntheses of the structural class of cochleamycins and macquarimicins. Part 3: EPC-syntheses of the β-keto lactone subunits and first attempts towards the syntheses of the pentacyclic antibiotics of this group

Practical EPC-syntheses of δ-substituted-β-keto δ-lactones, subunits of the cochleamycins and macquarimicins, are presented. In consequence Tietze's tandem reaction is employed to combine δ-allyl-β-keto δ-lactone with a hydrindene derivative, the second subunit of these acetogenic antibiotics. Model reactions for the final oxidative radical tandem cyclization reveal that the electrophilic radical cyclizes exclusively in exo-trig fashion. However, with the intended precursor of macquarimicin C allylic hydrogen abstraction thwarted the oxidative radical tandem cyclization.