24621-61-2Relevant academic research and scientific papers
Synthesis of (R)-1,3-butanediol by enantioselective oxidation using whole recombinant Escherichia coli cells expressing (S)-specific secondary alcohol dehydrogenase
Yamamoto, Hiroaki,Matsuyama, Akinobu,Kobayashi, Yoshinori
, p. 925 - 927 (2002)
The synthesis of (R)-1,3-butanediol (BDO) from its racemate was studied using whole cells of recombinant Escherichia coli expressing an (S)-specific secondary alcohol dehydrogenase (CpSADH) from Candida parapsilosis by enantioselective oxidation. Under the optimized conditions, the yield of (R)-1,3-BDO reached 72.6 g/l, with a molar recovery yield of 48.4% from a racemate of 15% and an optical purity of 95% ee.
The Absolute Configuration of 4-(Trichloromethyl)oxetan-2-one; A Case of Double Anchimeric Assistance with Inversion
Wynberg, Hans,Staring, Emiel G. J.
, p. 1181 - 1182 (1984)
It has been shown that the absolute configuration of the oxetan-2-one (1) is opposite to that of its hydrolysis product, S-(-)-malic acid (3).
Diastereoselective route to (2R,5S)- and (2S,5S)-2-methyl-1,6-dioxaspiro[4.5]decane, a pheromone component of the wasp Paravespula vulgaris
Zarbin, Paulo H. G.,De Oliveira, Alfredo R. M.,Delay, Carlos E.
, p. 6849 - 6851 (2003)
A diastereoselective approach to (2R,5S)- and (2S,5S)-2-methyl-1,6-dioxaspiro[4.5]decane 1 and 1a is described. The route starts with an alkylation reaction among the cyclopentanone N,N-dimethylhydrazone 6 and the chiral iodides (R)-3 or (S)-3, derived from the enantiomers of ethyl β-hydroxybutyrate, controlling the estereocenter at C-2 of the molecules. The alkylated products 7 and 7a were easily transformed into the 1,8-O-TBS-1,8-dihydroxy-5-nonanones 9 and 9a in four steps, and a subsequent stereoselective spiroketalization, in acidic media, afforded a Z:E mixture (1:2) of compounds 1 and 1a.
Preparation of enantiomerically pure 1,3-butanediol from threonine
Larcheveque,Mambu,Petit
, p. 2295 - 2300 (1991)
Enantiomerically pure R or S 1,3-butanediols were prepared in four steps from L to D threonine by nitrous deamination in the presence of bromide ion followed by esterification and reduction.
Efficient synthesis of the ketone body ester (R)-3-hydroxybutyryl-(R)-3-hydroxybutyrate and its (S,S) enantiomer
Budin, Noah,Higgins, Erin,DiBernardo, Anthony,Raab, Cassidy,Li, Chun,Ulrich, Scott
, p. 560 - 564 (2018)
The ketone body ester (R)-3-hydroxybutyryl-(R)-3-hydroxybutyrate and its (S,S) enantiomer were prepared in a short, operationally simple synthetic sequence from racemic β-butyrolactone. Enantioselective hydrolysis of β-butyrolactone with immobilized Candida antarctica lipase-B (CAL-B) results in (R)-β-butyrolactone and (S)-β-hydroxybutyric acid, which are easily converted to (R) or (S)-ethyl-3-hydroxybutyrate and reduced to (R) or (S)-1,3 butanediol. Either enantiomer of ethyl-3-hydroxybutyrate and 1,3 butanediol are then coupled, again using CAL-B, to produce the ketone body ester product. This is an efficient, scalable, atom-economic, chromatography-free, and low cost synthetic method to produce the ketone body esters.
Cloning and expression in Escherichia coli of a gene coding for a secondary alcohol dehydrogenase from Candida parapsilosis
Yamamoto, Hiroaki,Kawada, Naoki,Matsuyama, Akinobu,Kobayashi, Yoshinori
, p. 1051 - 1055 (1999)
A gene encoding a stereo-specific secondary alcohol dehydrogenase (CpSADH) that catalyzed the oxidation of (S)-1,3-BDO to 4-hydroxy-2-butanone was cloned from Candida parapsilosis. This CpSADH-gene consisted of 1,009 nucleotides coding for a protein with M, 35,964. A recombinant Escherichia coli JM109 strain harboring the expression plasmid, pKK-CPA1, produced (R)-1,3-BDO (93.5% ee, 94.7% yield) from the racemate without any additive to regenerate NAD+ from NADH.
Enantioselective Production of (S)-3-Hydroxybutyric Acid, (S)-1,3-Butanediol and (R)-1,3-Butanediol Using Methanol Yeast
Matsumura, Shuichi,Imafuku, Hiroshi,Takahashi, Yoshinori,Toshima, Kazunobu
, p. 251 - 254 (1993)
(S)-3-Hydroxybutyric acid and (S)-1,3-butanediol were obtained by the treatment of 1,3-butanediol with the resting cells of methanol yeast, Candida boidinii (IFO 10574). (R)-1,3-Butanediol was also obtained in high optical purity by the enantioselective reduction of 4-hydroxy-2-butanone in the presence of methanol using the same methanol yeast.
The Enantioface-differentiating Hydrogenation of the C=O Double Bond with Asymmetrically Modified Raney Nickel.XXXIII.The Preparation of (R)-and (S)-1,3-Butanediol from 4-Hydroxy-2-butanone
Murakami, Shigeki,Harada, Tadao,Tai, Akira
, p. 1356 - 1360 (1980)
The enantioface-differentianing hydrogenation of 4-hydroxy-2-butanone (I) to 1,3-butanediol (II) was conduced with asymmetrically modified metal catalysts.Among the modified catalysts examined, Raney nickel modified with a solution containing tartaric acid and NaBr (TA-NaBr-MRNi) gave the best results with respect to the optical and chemical yields. (R)-II, an optical purity of 69 percent was obtained in a quantitative chemical yeld by the use of (R,R)-TA-NaBr-MRNi. (S)-II was also obtained by the use of (S,S)-TA-NaBr-MRNi.A simple method for the preparation of optically pure (S)- and (R)-II from the hydrogenation product was also developed.
SYNTHESIS OF 3-HYDROXYBUTYRYL 3-HYDROXYBUTYRATE AND RELATED COMPOUNDS
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Paragraph 0308; 0317, (2021/04/02)
In various embodiments methods of preparing hydroxybutyryl 3-hydroxybutyrate and related compounds are provided along with methods of use thereof.
Conformational Dynamics-Guided Loop Engineering of an Alcohol Dehydrogenase: Capture, Turnover and Enantioselective Transformation of Difficult-to-Reduce Ketones
Liu, Beibei,Qu, Ge,Li, Jun-Kuan,Fan, Wenchao,Ma, Jun-An,Xu, Yan,Nie, Yao,Sun, Zhoutong
, p. 3182 - 3190 (2019/05/15)
Directed evolution of enzymes for the asymmetric reduction of prochiral ketones to produce enantio-pure secondary alcohols is particularly attractive in organic synthesis. Loops located at the active pocket of enzymes often participate in conformational changes required to fine-tune residues for substrate binding and catalysis. It is therefore of great interest to control the substrate specificity and stereochemistry of enzymatic reactions by manipulating the conformational dynamics. Herein, a secondary alcohol dehydrogenase was chosen to enantioselectively catalyze the transformation of difficult-to-reduce bulky ketones, which are not accepted by the wildtype enzyme. Guided by previous work and particularly by structural analysis and molecular dynamics (MD) simulations, two key residues alanine 85 (A85) and isoleucine 86 (I86) situated at the binding pocket were thought to increase the fluctuation of a loop region, thereby yielding a larger volume of the binding pocket to accommodate bulky substrates. Subsequently, site-directed saturation mutagenesis was performed at the two sites. The best mutant, where residue alanine 85 was mutated to glycine and isoleucine 86 to leucine (A85G/I86L), can efficiently reduce bulky ketones to the corresponding pharmaceutically interesting alcohols with high enantioselectivities (～99% ee). Taken together, this study demonstrates that introducing appropriate mutations at key residues can induce a higher flexibility of the active site loop, resulting in the improvement of substrate specificity and enantioselectivity. (Figure presented.).
