497-09-6Relevant articles and documents
Enantioselective Reductive Oligomerization of Carbon Dioxide into l-Erythrulose via a Chemoenzymatic Catalysis
Bontemps, Sébastien,Clapés, Pere,Desmons, Sarah,Dumon, Claire,Fauré, Régis,Grayson-Steel, Katie,Hurtado, John,Nu?ez-Dallos, Nelson,Vendier, Laure
supporting information, p. 16274 - 16283 (2021/10/12)
A cell-free enantioselective transformation of the carbon atom of CO2has never been reported. In the urgent context of transforming CO2into products of high value, the enantiocontrolled synthesis of chiral compounds from CO2would be highly desirable. Using an original hybrid chemoenzymatic catalytic process, we report herein the reductive oligomerization of CO2into C3(dihydroxyacetone, DHA) and C4(l-erythrulose) carbohydrates, with perfect enantioselectivity of the latter chiral product. This was achieved with the key intermediacy of formaldehyde. CO2is first reduced selectively by 4e-by an iron-catalyzed hydroboration reaction, leading to the isolation and complete characterization of a new bis(boryl)acetal compound derived from dimesitylborane. In an aqueous buffer solution at 30 °C, this compound readily releases formaldehyde, which is then involved in selective enzymatic transformations, giving rise either (i) to DHA using a formolase (FLS) catalysis or (ii) to l-erythrulose with a cascade reaction combining FLS and d-fructose-6-phosphate aldolase (FSA) A129S variant. Finally, the nature of the synthesized products is noteworthy, since carbohydrates are of high interest for the chemical and pharmaceutical industries. The present results prove that the cell-freede novosynthesis of carbohydrates from CO2as a sustainable carbon source is a possible alternative pathway in addition to the intensely studied biomass extraction andde novosyntheses from fossil resources.
Electrochemical Activation of Galactose Oxidase: Mechanistic Studies and Synthetic Applications
Fryszkowska, Anna,Klapars, Artis,Marshall, Nicholas,Ruccolo, Serge,Strotman, Neil A.,Zhang, Shaoguang
, p. 7270 - 7280 (2021/06/30)
The enzyme galactose oxidase (GOase) is a copper radical oxidase that catalyzes the aerobic oxidation of primary alcohols to the aldehydes and has been utilized to that end in large-scale pharmaceutical processes. To maintain its catalytic activity and ensure high substrate conversion, GOase needs to be continuously (re)activated by 1e- oxidation of the constantly formed out-of-cycle species (GOasesemi) to the catalytically active state (GOaseox). In this work, we report an electrochemical activation method for GOase that replaces the previously used expensive horseradish peroxidase activator in a GOase-catalyzed oxidation reaction. First, the formation of GOaseox of a specifically engineered variant via nonenzymatic oxidation of GOasesemi was studied by UV-vis spectroscopy. Second, electrochemical oxidation of GOase by mediators was studied using cyclic voltammetry. The electron-transfer rates between GOase and various mediators at different pH values were determined, showing a dependence on both the redox potential of the mediator and the pH. This observation suggests that the oxidation of GOase by mediators at pH 7-9 likely occurs via a concerted proton-coupled electron-transfer (PCET) mechanism under anaerobic conditions. Finally, this electrochemical GOase activation method was successfully applied to the development of a bioelectrocatalytic GOase-mediated aerobic oxidation of benzyl alcohol derivatives, cinnamyl alcohol, and aliphatic polyols, including the desymmetrizing oxidation of 2-ethynylglycerol, a key step in the biocatalytic cascade used to prepare the promising HIV therapeutic islatravir.
Convergent in situ Generation of Both Transketolase Substrates via Transaminase and Aldolase Reactions for Sequential One-Pot, Three-Step Cascade Synthesis of Ketoses
Lorillière, Marion,Guérard-Hélaine, Christine,Gefflaut, Thierry,Fessner, Wolf-Dieter,Clapés, Pere,Charmantray, Franck,Hecquet, Laurence
, p. 812 - 817 (2019/12/27)
We describe an efficient three-enzyme, sequential one-pot cascade reaction where both transketolase substrates are generated in situ in a convergent fashion. The nucleophilic donor substrate hydroxypyruvate was obtained from l-serine and pyruvate by a transaminase-catalyzed reaction. In parallel, three different (2S)-α-hydroxylated aldehydes, l-glyceraldehyde, d-threose, and l-erythrose, were generated as electrophilic acceptors from simple achiral compounds glycolaldehyde and formaldehyde by d-fructose-6-phosphate aldolase catalysis. The compatibility of the three enzymes was studied in terms of temperature, enzyme ratio and substrate concentration. The efficiency of the process relied on the irreversibility of the transketolase reaction, driving a shift of the reversible transamination reaction and securing the complete conversion of all substrates. Three valuable (3S,4S)-ketoses, l-ribulose, d-tagatose, and l-psicose were obtained in good yields with high diastereoselectivity.
Phosphorylation Catalyzed by Dihydroxyacetone Kinase
Gauss, Dominik,Sánchez-Moreno, Israel,Oroz-Guinea, Isabel,García-Junceda, Eduardo,Wohlgemuth, Roland
supporting information, p. 2892 - 2895 (2018/05/15)
Site- and enantioselective kinases have been very useful catalysts for biocatalytic phosphorylations in straightforward syntheses of phosphorylated metabolites. Biocatalytic phosphorylations catalyzed by recombinant dihydroxyacetone kinase beyond the dihydroxyacetone substrate have been investigated with quantitative 31P NMR spectroscopy using pyruvate-kinase-catalyzed ATP regeneration. A nearly 100 % conversion of d-glyceraldehyde to d-glyceraldehyde 3-phosphate has been found. Interestingly, with pure l-glyceraldehyde as substrate, practically no formation of l-glyceraldehyde 3-phosphate was observed.
Prebiotic synthesis of 2-deoxy-d-ribose from interstellar building blocks promoted by amino esters or amino nitriles
Steer, Andrew M.,Bia, Nicolas,Smith, David K.,Clarke, Paul A.
supporting information, p. 10362 - 10365 (2017/09/25)
Understanding the prebiotic genesis of 2-deoxy-d-ribose, which forms the backbone of DNA, is of crucial importance to unravelling the origins of life, yet remains open to debate. Here we demonstrate that 20 mol% of proteinogenic amino esters promote the selective formation of 2-deoxy-d-ribose over 2-deoxy-d-threopentose in combined yields of ≥4%. We also demonstrate the first aldol reaction promoted by prebiotically-relevant proteinogenic amino nitriles (20 mol%) for the enantioselective synthesis of d-glyceraldehyde with 6% ee, and its subsequent conversion into 2-deoxy-d-ribose in yields of ≥ 5%. Finally, we explore the combination of these two steps in a one-pot process using 20 mol% of an amino ester or amino nitrile promoter. It is hence demonstrated that three interstellar starting materials, when mixed together with an appropriate promoter, can directly lead to the formation of a mixture of higher carbohydrates, including 2-deoxy-d-ribose.
Synthesis of dihydrosterculic acid-based monoglucosyl diacylglycerol and its analogues and their biological evaluation
Srikanth, Vudhgiri,Prasad,Poornachandra,Phani Babu,Ganesh Kumar,Jagadeesh,Jala, Ram Chandra Reddy
, p. 134 - 145 (2016/01/16)
In the present study, Lactobacillus plantarum glycolipid (GL1) molecule in β-configuration and its fatty acid analogues were synthesized using trichloroacetimidate methodology. The β-configuration of the GL1 molecule was unambiguously assigned by NMR studies using 2D-ROESY (NOE) and J-coupling analysis. Dihydrosterculic acid was synthesized using Furukawa's reagent and the selective esterification of dihydrosterculic acid at C-3 position of glycerol was achieved with EDC-HCl at 0 °C. In vitro cytotoxicity of the GL1 molecule and its fatty acid analogues was evaluated against DU145, A549, SKOV3 and MCF7 cell lines. Among all the synthesized molecules, the GL1 molecule and compound 7d showed moderate activity, while the compound 7b showed promising activity against all the tested cell lines with IC50 values of 20.1, 18.2, 19.1 and 17.6 ?1/4M, respectively. In addition, all tested compounds showed poor cytotoxicity against normal HUVEC cells. The MCF7 cells when treated with compound 7b showed lower bromodeoxyuridine incorporation levels as compared to untreated cells, suggesting that the compound 7b was highly effective and inhibited the cell proliferation. In addition, the compounds showed significant increase in caspases 3 and 9 levels by inducing apoptosis in MCF 7 cells.
Facile enzymatic synthesis of ketoses
Wen, Liuqing,Huang, Kenneth,Wei, Mohui,Meisner, Jeffrey,Liu, Yunpeng,Garner, Kristina,Zang, Lanlan,Wang, Xuan,Li, Xu,Fang, Junqiang,Zhang, Houcheng,Wang, Peng George
supporting information, p. 12654 - 12658 (2015/10/28)
Studies of rare ketoses have been hampered by a lack of efficient preparation methods. A convenient, efficient, and cost-effective platform for the facile synthesis of ketoses is described. This method enables the preparation of difficult-to-access ketopentoses and ketohexoses from common and inexpensive starting materials with high yield and purity and without the need for a tedious isomer separation step. A spoonful of sugar: A convenient, efficient, and cost-effective platform for the facile synthesis of ketoses is described. This method, which involves a one-pot mulitenzyme (OPME) reaction, enables the preparation of rare ketopentoses and ketohexoses from common and inexpensive starting materials with high yield and purity and without the need for a tedious isomer separation step.
A likely possible origin of homochirality in amino acids and sugars on prebiotic earth
Breslow, Ronald
supporting information; scheme or table, p. 2028 - 2032 (2011/05/09)
For life to start on earth and elsewhere, it is critical that the building blocks - amino acids and sugars - be in predominant homochiral form. Over the past century, the origin of terrestrial prebiotic homochirality has been the subject of many speculations. In this Letter I summarize the experimental evidence for ways in which some meteoritic components could have led to the dominance of l amino acids and d sugars on earth, and the most likely way in which the original chiral excesses in the meteorites were formed.
Engineering stereocontrol into an aldolase-catalysed reaction
Lamble, Henry J.,Danson, Michael J.,Hough, David W.,Bull, Steven D.
, p. 124 - 126 (2007/10/03)
A novel thermostable aldolase has been developed for synthetic application, and substrate engineering has been used to induce stereocontrol into aldol reactions of this naturally-promiscuous enzyme.
One-pot synthesis of L-fructose using coupled multienzyme systems based on rhamnulose-1-phosphate aldolase
Franke, Dirk,Machajewski, Timothy,Hsu, Che-Chang,Wong, Chi-Huey
, p. 6828 - 6831 (2007/10/03)
Two methods have been developed for the highly efficient enzymatic synthesis of L-fructose: one is based on rhamnulose-1-phosphate aldolase and acid phosphatase using racemic glyceraldehyde and dihydroxyacetone phosphate as substrates; the other is to gen
