78183-56-9

Usage

Uses

Used in Chemical Reactions:
(3S)-2-Butanone, 3-hydroxyis used as a reagent in various chemical reactions for its reactive nature, allowing for the synthesis of different compounds in laboratories.
Used in Biochemical Research:
(3S)-2-Butanone, 3-hydroxymay be used as a research tool in biochemical studies to understand its potential roles in various biochemical functions and interactions.

Upstream product

• 1029272-42-1 (2R,3S)-2,3-butanediol 
• 75-07-0 acetaldehyde 
• 127-17-3 2-oxo-propionic acid 
• 88376-46-9 (S)-3-methylbut-3-en-2-ol 
• 73346-75-5 (R)-2,2,4r,5t-tetramethyl-[1,3]dioxolane 
• 86452-30-4 ethyl (E)‐4‐hydroxy‐3‐methylpent‐2‐enoate 
• 112449-88-4 3-Methyl-4-phenylsulfanylbut-3-en-2-ol 
• 173948-58-8 (S,E)-3-Methyl-4-phenylsulfonylbut-3-en-2-ol 
• 19132-06-0 (2S,3S)-butane-2,3-diol 
• 101396-19-4 2-((S)-1-hydroxyethyl)-2-methyl-1,3-dithiane 
• 513-86-0 3-hydroxy-2-butanon 
• 431-03-8 dimethylglyoxal 
• 113-24-6 sodium pyruvate 
• 97203-22-0 (-)-(S)-3-(phenylmethoxy)-2-butanone 

Downstream Products

• 88376-42-5 hydrogen phthalate of (S)-acetoin 
• 19132-06-0 (2S,3S)-butane-2,3-diol 
• 1029272-42-1 (2R,3S)-2,3-butanediol 
• 167777-72-2 (-)-S-3-<oxy>-2-butanone 
• 1093653-29-2 C₇H₉NO₃ 

Relevant academic research and scientific papers

Efficient (3S)-acetoin and (2S, 3S)-2, 3-butanediol production from meso-2, 3-butanediol using whole-cell biocatalysis

(3S)-Acetoin and (2S, 3S)-2, 3-butanediol are important platform chemicals widely applied in the asymmetric synthesis of valuable chiral chemicals. However, their production by fermentative methods is difficult to perform. This study aimed to develop a whole-cell biocatalysis strategy for the production of (3S)-acetoin and (2S, 3S)-2, 3-butanediol from meso-2, 3-butanediol. First, E. coli co-expressing (2R, 3R)-2, 3-butanediol dehydrogenase, NADH oxidase and Vitreoscilla hemoglobin was developed for (3S)-acetoin production from meso-2, 3-butanediol. Maximum (3S)-acetoin concentration of 72.38 g/L with the stereoisomeric purity of 94.65% was achieved at 24 h under optimal conditions. Subsequently, we developed another biocatalyst co-expressing (2S, 3S)-2, 3-butanediol dehydrogenase and formate dehydrogenase for (2S, 3S)-2, 3-butanediol production from (3S)-acetoin. Synchronous catalysis together with two biocatalysts afforded 38.41 g/L of (2S, 3S)-butanediol with stereoisomeric purity of 98.03% from 40 g/L meso-2, 3-butanediol. These results exhibited the potential for (3S)-acetoin and (2S, 3S)-butanediol production from meso-2, 3-butanediol as a substrate via whole-cell biocatalysis.

Enhanced production of optical (: S)-acetoin by a recombinant Escherichia coli whole-cell biocatalyst with NADH regeneration

Acetoin is an important platform chemical with a variety of applications in foods, cosmetics, chemical synthesis, and especially in the asymmetric synthesis of optically active pharmaceuticals. It is also a useful breath biomarker for early lung cancer diagnosis. In order to enhance production of optical (S)-acetoin and facilitate this building block for a series of chiral pharmaceuticals derivatives, we have developed a systematic approach using in situ-NADH regeneration systems and promising diacetyl reductase. Under optimal conditions, we have obtained 52.9 g L-1 of (S)-acetoin with an enantiomeric purity of 99.5% and a productivity of 6.2 g (L h)-1. The results reported in this study demonstrated that the production of (S)-acetoin could be effectively improved through the engineering of cofactor regeneration with promising diacetyl reductase. The systematic approach developed in this study could also be applied to synthesize other optically active α-hydroxy ketones, which may provide valuable benefits for the study of drug development.

Elucidation of the enantioselective cyclohexane-1,2-dione hydrolase catalyzed formation of (S)-acetoin

Thiamine diphosphate (ThDP) dependent enzymes catalyze the formation of acetoin (3-hydroxybutan-2-one) through one of three different pathways: homocoupling of pyruvate, homocoupling of acetaldehyde, or cross-coupling of acetaldehyde (as acceptor) and pyruvate (as donor). The enantioselectivity of the resulting acetoin is highly dependent on the particular enzyme. We established that ThDP-dependent cyclohexane-1,2-dione hydrolase (CDH) is able to form (S)-acetoin with particularly high enantioselectivity (up to 95 % ee) by all three pathways. Mechanistic studies utilizing 13C-labeled substrates revealed an unprecedented non-acetolactate pathway for the homocoupling of pyruvate, which explains the high enantioselectivity in the CDH-catalyzed formation of (S)-acetoin. Differentiating hydrolases: Investigating thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase (CDH) catalyzed homocoupling of 13C-labeled [1,2]-13C-pyruvate to (S)-[2,3]-13C-acetoin reveals a non-acetolactate pathway, which explains the high enantioselectivity of this reaction (up to 93 % ee). CDH also catalyzes the formation of (S)-acetoin by the cross-coupling of pyruvate and acetaldehyde and the homocoupling of acetaldehyde.

Extended reaction scope of thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase: From C-C bond cleavage to C-C bond ligation

ThDP-dependent cyclohexane-1,2-dione hydrolase (CDH) catalyzes the CC bond cleavage of cyclohexane-1,2-dione to 6-oxohexanoate, and the asymmetric benzoin condensation between benzaldehyde and pyruvate. One of the two reactivities of CDH was selectively knocked down by mutation experiments. CDH-H28A is much less able to catalyze the CC bond formation, while the ability for CC bond cleavage is still intact. The double variant CDH-H28A/N484A shows the opposite behavior and catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol. Several acyloins of tertiary alcohols are formed with 54-94% enantiomeric excess. In addition to pyruvate, methyl pyruvate and butane-2,3-dione are alternative donor substrates for CC bond formation. Thus, the very rare aldehyde-ketone cross-benzoin reaction has been solved by design of an enzyme variant.

Enantioselective hydrogenation of activated ketones in the presence of Pt-cinchona catalysts. Is the proton transfer concept valid?

Experimental evidences related to the proton transfer in the catalytic system Pt-cinchona alkaloids for enantioselective hydrogenation of activated ketones were collected and analyzed. Both new and earlier results indicate that in aprotic media direct transfer of proton from platinum to the substrate with the involvement of quinuclidine nitrogen as a general rule can be questioned.

α-Hydroxy-β-keto acid rearrangement-decarboxylation: Impact on thiamine diphosphate-dependent enzymatic transformations

The thiamine diphosphate (ThDP) dependent MenD catalyzes the reaction of α-ketoglutarate with pyruvate to selectively form 4-hydroxy-5-oxohexanoic acid 2, which seems to be inconsistent with the assumed acyl donor role of the physiological substrate α-KG. In contrast the reaction of α-ketoglutarate with acetaldehyde gives exclusively the expected 5-hydroxy-4-oxo regioisomer 1. These reactions were studied by NMR and CD spectroscopy, which revealed that with pyruvate the observed regioselectivity is due to the rearrangement-decarboxylation of the initially formed α-hydroxy-β-keto acid rather than a donor-acceptor substrate role variation. Further experiments with other ThDP-dependent enzymes, YerE, SucA, and CDH, verified that this degenerate decarboxylation can be linked to the reduced enantioselectivity of acyloins often observed in ThDP-dependent enzymatic transformations.

Biocatalytic production of alpha-hydroxy ketones and vicinal diols by yeast and human aldo-keto reductases

The α-hydroxy ketones are used as building blocks for compounds of pharmaceutical interest (such as antidepressants, HIV-protease inhibitors and antitumorals). They can be obtained by the action of enzymes or whole cells on selected substrates, such as diketones. We have studied the enantiospecificities of several fungal (AKR3C1, AKR5F and AKR5G) and human (AKR1B1 and AKR1B10) aldo-keto reductases in the production of α-hydroxy ketones and diols from vicinal diketones. The reactions have been carried out with pure enzymes and with an NADPH-regenerating system consisting of glucose-6-phosphate and glucose-6-phosphate dehydrogenase. To ascertain the regio and stereoselectivity of the reduction reactions catalyzed by the AKRs, we have separated and characterized the reaction products by means of a gas chromatograph equipped with a chiral column and coupled to a mass spectrometer as a detector. According to the regioselectivity and stereoselectivity, the AKRs studied can be divided in two groups: one of them showed preference for the reduction of the proximal keto group, resulting in the S-enantiomer of the corresponding α-hydroxy ketones. The other group favored the reduction of the distal keto group and yielded the corresponding R-enantiomer. Three of the AKRs used (AKR1B1, AKR1B10 and AKR3C1) could produce 2,3-butanediol from acetoin. We have explored the structure/function relationships in the reactivity between several yeast and human AKRs and various diketones and acetoin. In addition, we have demonstrated the utility of these AKRs in the synthesis of selected α-hydroxy ketones and diols.

Silica supported rhodium metal nanoparticles stabilized with (-)-DIOP. Effect of ligand concentration and metal loading on the enantioselective hydrogenation of ketones

Supported nanoparticles (NPs) in presence of chiral ligand (L) were synthesized for their use in enantioselective hydrogenation reactions. Catalysts were obtained by chemical reduction from rhodium chloride hydrate, RhCl 3×3H2O, in presence of (-)-DIOP ligand ((4R,5R)-4,5-Bis(diphenylphosphino-methyl)- 2,2-dimethyl-1,3-dioxolane) that allows to control NPs growing and to obtain solids having chiral surfaces. Chirally stabilized rhodium NPs on SiO2 were characterized using techniques such as: TEM, electron diffraction, EDS, nitrogen adsorption-desorption isotherms and XPS. This work includes the study of some variables such as metal loading and ligand concentration and their effect in metal core sizes, catalytic activity and enantioselectivity. Catalysts properties have also been evaluated in the hydrogenation of substrates: acetophenone (AP), 1-phenyl-1,2-propanedione (PPD), 3,4-hexanedione (HD), 2,3-butanedione (BD) and ethyl pyruvate (EP) as reaction test. Ligand plays a fundamental role in the synthesis of NPs and enantioselectivity in hydrogenations reactions. That is, due to it generates metal particle size 5.8 nm compared with unstabilized systems that generate average diameter around 14 nm. Results indicate increased activity in catalytic systems obtained from the stabilization of NPs. Enantioselectivity levels reach values up to 53% due to the chiral ligand is on the catalysts surface.

Enantioselective Intermolecular Aldehyde Ketone Cross-Coupling through an Enzymatic Carboligation Reaction

(Figure Presented) Happy new YerE: The first example of the title reaction is presented using a ThDPdependent enzyme catalyst. The substrate tolerance of the enzyme is very broad and includes cyclic and open-chain ketones, as well as diketones and a- and β-ketoesters as acceptor substrates. The absolute configurations of two enzymatic products were determined by single-crystal structure analysis.

Rhodotorula minuta-mediated bioreduction of 1,2-diketones

The reduction of cyclic and acyclic 1,2-diketones was investigated by employing whole cells of the yeast Rhodotorula minuta as biocatalyst. The reactions showed a variable degree of regio- and enantioselectivity depending on the nature of the substrate. In the case of cyclic diketones, the reduction afforded a mixture of diastereomeric diols only. The reduction of acyclic diketones allowed production of both the hydroxy ketone and the diol, in a two-step reaction. The first step was highly regio- and stereoselective, affording the hydroxy ketone of (S)-configuration with high enantiomeric excess. After longer reaction times the corresponding (S,S)-diols were obtained in high yield and diastereomeric excess.