One‐Pot Cascade Reactions using Fructose‐6‐phosphate Aldolase: Efficient Synthesis of <scp>D</scp>‐Arabinose 5‐Phosphate, <scp>D</scp>‐Fructose 6‐Phosphate and Analogues

Sánchez-Moreno, Israel; Hélaine, Virgil; Poupard, N.; Charmantray, Franck; Légeret, Bertrand; Hecquet, Laurence; García‐Junceda, Eduardo; Wohlgemuth, Roland; Guérard-Hélaine, Christine; Lemaire, Marielle

doi:10.1002/adsc.201200150

Cited by 51 publications

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“…4.1.2 from E. coli ). The enzyme/LDH ratios were fixed according to the specific activities of the enzymes and the results described for the non‐immobilized system involved to prepare d ‐F6P . The results obtained for the four enzymes are gathered in Table .…”

Section: Methodsmentioning

confidence: 99%

“…First, DHAP is formed by phosphorylation of DHA by using ATP‐dependent DHAK. Then, isomerization of DHAP into d ‐G3P occurs under catalysis of TPI . Finally, aldolization between DHA and d ‐G3P by using FSA A129S shifts the equilibrium (Scheme ) to the formation of d ‐F6P.…”

Section: Methodsmentioning

confidence: 99%

“…The synthesis of DHAP by using free or immobilized enzymes was realized as described previously with minor modifications . DHA (0.4 mmol), phosphoenolpyruvate (PEP, 0.32 mmol), ATP (52 μmol), and MgCl 2 (10 m m ) were mixed in the reaction medium.…”

Section: Methodsmentioning

confidence: 99%

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Design of Artificial Metabolisms in Layered Nanomaterials for the Enzymatic Synthesis of Phosphorylated Sugars

et al. 2015

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This manuscript is dedicated to Wolf-Dieter "Woody" Fessneront he occasion of his 60th birthday.Biohybrid nanoreactors operating in one-pot cascade reactions were designed by co-immobilizationofe nzymes in an inorganic layered matrix,n amely,l ayered double hydroxides.T hese biohybrid systems were devoted to prepare dihydroxyacetone phosphate (DHAP) and phosphorylated sugars throughs tereoselectiveC ÀCb ond formation. In the first system,t wo kinases were exploited for the in situ generation of DHAP.I ncreasing the complexity,t he second nano-bioreactorc ombined up to four enzymest ol ead to d-fructose-6-phosphate from the aldol-catalyzed addition of dihydroxyacetone to d-glyceraldehyde-3-phosphate generated in situ from DHAP.T he biohybrid catalysts howedt he same reactionr ate as that of the free enzymes and was reusable.Ta ndema nd cascade reactions were highlighted by Trost et al. in 2008 [1] as being of fundamentali mportance to develop greener syntheses. Biocatalysis takes am ajor place in this field, in particular enzymatic cascades,w hich create artificial pathways for the preparation of chiral or complex chemicals.[2] This emerging concept was recently termed "systemb iocatalysis" by Fessner.[3] Nature can be mimicked by designing artificial metabolic and non-naturalb iocatalytic pathways in vitro. In such multienzymatics ystems, enzymes are brought together in the same reactionv essel, in which the product of one enzymei st he substrate of the other.T he reactionp arameters (e.g.,p H, enzyme quantity,s ubstrate concentration, cosolvent, temperature, etc.) are easier to control than in in vivo systems and can be adjusted to reach high yields and purities.[4-6] To approachn aturals ystemsf or which the cooperating enzymes are organized in specific assemblies leading, in some cases, to ac hanneling effect,t he artificial metabolic pathways can be immobilized following different strategies. They have been nicely reviewed by Schoffelen et al.[5] The strategies are classified in order of increasing controlo ft he enzyme organization: random co-immobilization to as olid support (e.g.,a garose, [7] chitin, [8] nylon, [8] polystyrene, [9] polyvinyl chloride [10] )o rn anoparticles( e.g.,g oldn anoparticles, [11] sol-gelm atrix [12] ), sequential immobilization in microfluidic channels, positional immobilization on DNA nanostructures, site-specific enzymei mmobilization, and finally scaffold-free cross-linking.In this work, we aim to design cascader eactions for the enzymatics ynthesis of phosphorylated sugars followingt he random co-immobilizationo fe nzymes embedded in layered double hydroxide (LDH) nanoplatelets. Indeed LDHs, M II 1Àx M III x (OH) 2 X x/q ·n H 2 O( Supporting Information, Scheme S1), owing to their two-dimensional structure, physicochemical properties, and controllable nanoplateleta ggregation, [13] offer as uitable microenvironment that favorsahigh loading of enzymes, an increase in their stability, andp reservation of their activity. [14] In the course of our work on green by design,e fficie...

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Design of Artificial Metabolisms in Layered Nanomaterials for the Enzymatic Synthesis of Phosphorylated Sugars

et al. 2015

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“…In a very recent contribution, a further enzymatic step was incorporated into the cascade to provide DHAP from DHA. The additional step was made by means of a direct phosphorylation reaction catalyzed by a dihydroxyacetone kinase (DHAK) including an ATP regeneration system, thus avoiding the usage of expensive DHAP . Also, this modular cascade has been successfully used for the preparation of phosphorylated sugars, which are synthetically useful for the preparation of biologically relevant compounds including antibiotics, nucleosides, oligosaccharides, etc.…”

Section: Biomimetic Approaches Using Aldolasesmentioning

confidence: 99%

Recent Developments in the Preparation of Carbohydrate Derivatives from Achiral Building Blocks by using Aldolases

Busto

2016

ChemCatChem

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The central role of carbohydrates in medicinal chemistry has stimulated intensive research in the last few years to develop simpler and more efficient routes for their preparation. Among them, routes starting from simple and achiral building blocks have received particular attention considering their efficiency in terms of cost process and atom economy. Recent developments in the field of biocatalytic asymmetric aldol reactions have allowed the preparation of complex carbohydrate derivatives with high degrees of sophistication (up to five chiral centers). Starting from simple and achiral building blocks, such as dihydroxyacetone, glycolaldehyde, and formaldehyde, the reactions were found to proceed under complete stereocontrol. The aim of this review is to cover the most significant advances in the preparation of carbohydrate derivatives through asymmetric aldol reactions within the last five years. Selected examples include the preparation of rare natural d‐sugars such as d‐psicose, non‐natural l‐sugars and azasugars, as well as iminocyclitols or homo(iminocyclitols), C‐arylcarbohydrates, etc.

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“…Phosphorylated metabolites such as L-glyceraldehyde-3-phosphate (L-GAP) are synthetically useful to design in vitro single-pot cascade biocatalytic reaction sequences using enzymes such as aldolases or transketolases [6][7][8][9][10]. L-GAP has been described to have a bactericidal effect on Escherichia coli while D-GAP does not have the same effect [11].…”

Section: Introductionmentioning

confidence: 99%

Bioreaction Engineering Leading to Efficient Synthesis of L‐Glyceraldehyd‐3‐Phosphate

Molla

Kinfu

Chow

et al. 2017

Biotechnology Journal

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Enantiopure L-glyceraldehyde-3-phosphate (L-GAP) is a useful building block in natural biological and synthetic processes. A biocatalytic process using glycerol kinase from Cellulomonas sp. (EC 2.7.1.30) catalyzed phosphorylation of L-glyceraldehyde (L-GA) by ATP is used for the synthesis of L-GAP. L-GAP has a half-life of 6.86 h under reaction conditions. The activity of this enzyme depends on the Mg to ATP molar ratio showing maximum activity at the optimum molar ratio of 0.7. A kinetic model is developed and validated showing a 2D correlation of 99.9% between experimental and numerical data matrices. The enzyme exhibits inhibition by ADP, AMP, methylglyoxal and Ca , but not by L-GAP and inorganic orthophosphate. Moreover, equal amount of Ca exerts a different degree of inhibition relative to the activity without the addition of Ca depending on the Mg to ATP molar ratio. If the Mg to ATP molar ratio is set to be at the optimum value or less, inorganic hexametaphosphate (PPi6) suppresses the enzyme activity; otherwise PPi6 enhances the enzyme activity. Based on reaction engineering parameters such as conversion, selectivity and specific productivity, evaluation of different reactor types reveals that batchwise operation via stirred-tank reactor is the most efficient process for the synthesis of L-GAP.

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One‐Pot Cascade Reactions using Fructose‐6‐phosphate Aldolase: Efficient Synthesis of D‐Arabinose 5‐Phosphate, D‐Fructose 6‐Phosphate and Analogues

Cited by 51 publications

References 55 publications

Design of Artificial Metabolisms in Layered Nanomaterials for the Enzymatic Synthesis of Phosphorylated Sugars

Design of Artificial Metabolisms in Layered Nanomaterials for the Enzymatic Synthesis of Phosphorylated Sugars

Recent Developments in the Preparation of Carbohydrate Derivatives from Achiral Building Blocks by using Aldolases

Bioreaction Engineering Leading to Efficient Synthesis of L‐Glyceraldehyd‐3‐Phosphate

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