A Flexible Polyphosphate‐Driven Regeneration System for Coenzyme A Dependent Catalysis

Mordhorst, Silja; Maurer, Alice; Popadić, Désirée; Brech, Johanna; Andexer, Jun.-Prof. Dr. Jennifer N.

doi:10.1002/cctc.201700848

Cited by 33 publications

(27 citation statements)

References 40 publications

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“…PPK1 and PPK2 enzymes are structurally and sequentially unrelated. PPK2 enzymes are highly efficient biocatalysts in cofactor regeneration systems for adenosine 5′‐triphosphate (ATP)‐dependent processes . The PPK2 family can be phylogenetically divided into three classes (Scheme ) .…”

Section: Methodsmentioning

confidence: 99%

Several Polyphosphate Kinase 2 Enzymes Catalyse the Production of Adenosine 5′‐Polyphosphates

et al. 2019

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Polyphosphate kinases (PPKs) are involved in many metabolic processes; enzymes of the second family (PPK2) are responsible for nucleotide synthesis fuelled by the consumption of inorganic polyphosphate. They catalyse the phosphorylation of nucleotides with various numbers of phosphate residues, such as monophosphates or diphosphates. Hence, these enzymes are promising candidates for cofactor regeneration systems. Besides adenosine 5′‐triphosphate, PPK2s also catalyse the synthesis of highly phosphorylated nucleotides in vitro, as shown here for adenosine 5′‐tetraphosphate and adenosine 5′‐pentaphosphate. These unusually phosphorylated adenosine 5′‐polyphosphates add up to 50 % of the whole adenosine nucleotides in the assay. The two new products were chemically synthesised to serve as standards and compared with the two enzymatically produced compounds by high‐performance ion chromatography and 31P NMR analysis. This study shows that PPK2s are highly suitable for biocatalytic synthesis of different phosphorylated nucleotides.

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Section: Methodsmentioning

confidence: 99%

Several Polyphosphate Kinase 2 Enzymes Catalyse the Production of Adenosine 5′‐Polyphosphates

et al. 2019

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“…Despite the regeneration modules for these two cofactors can be recruited to lower the input of NAD/CoA, the cost of these expensive cofactors will be greatly enhanced when the system is scaled up. In addition, the instability of NAD and CoA can lower the efficiency of the reaction system ,…”

Section: Figurementioning

confidence: 99%

Stoichiometric Regeneration of ATP by A NAD(P)/CoA‐free and Phosphate‐balanced In Vitro Synthetic Enzymatic Biosystem

et al. 2018

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The regeneration of adenosine triphosphate is crucial for establishing a cost‐effective biosystem in which energy‐dependent processes are involved. Here, an in vitro synthetic enzymatic biosystem was designed to utilize low‐cost starch‐based material as energy source for the stoichiometric regeneration of ATP. This system required neither NAD(P) nor coenzyme A, and theoretically produced 3 ATPs per glucose equivalent of starch. When integrated with the L‐theanine‐producing enzymatic reaction which consumes 1 ATP to generate 1 L‐theanine molecule, our system resulted in a near‐theoretical yield of 2.94 L‐theanine per glucose equivalent. Furthermore, inorganic phosphate concentration of the system was nearly constant throughout the reaction period, suggesting the homeostatic reaction environment for enzymatic processes. This work provides a useful strategy for cost‐effective ATP regeneration which facilitates the production of ATP‐dependent value‐added chemicals.

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“…The CL‐NAT cascade has also been applied in vitro by Andexer and co‐workers . In order to enable these systems in vitro , the issue of recycling of the requisite ATP cofactor of the CL must be considered.…”

Section: Atp‐dependent Systemsmentioning

confidence: 99%

Enzyme‐Catalysed Synthesis of Secondary and Tertiary Amides

Petchey

Grogan

2019

Adv Synth Catal

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Thes ynthesis of the amide bondb etween an amine andacarboxylic acid is one of the most significant reactions in industrial pharmaceutical synthesis.D espite the apparents implicityo fs ynthetic methodsf or amide bond formation, many of these are disadvantaged by their requirementf or toxic or hazardous reagents for the activation of the acid component, or poora tom economy resulting from the need for stoichiometric amountso fc oupling reagents.I nt his context, biocatalysis hase merged as an alternative catalytic method for amide bond formation, presenting the advantages of both environmentally benign reagents andc onditions and also atom economy.I nthis review we detail developments in the enzyme-catalysed preparation of secondary andt ertiary amides for the synthesis of pharmaceutical-type molecules andr eview the applications of hydrolases,s uch as lipasesa nd penicillina cylases, to these reactions.W ea lso summarise the activity of ATP-dependent enzymesf or amide bondf ormation and assess their potentialf or the preparative synthesis of amidesf rom carboxylic acids and amines in aqueous media.

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A Flexible Polyphosphate‐Driven Regeneration System for Coenzyme A Dependent Catalysis

Cited by 33 publications

References 40 publications

Several Polyphosphate Kinase 2 Enzymes Catalyse the Production of Adenosine 5′‐Polyphosphates

Several Polyphosphate Kinase 2 Enzymes Catalyse the Production of Adenosine 5′‐Polyphosphates

Stoichiometric Regeneration of ATP by A NAD(P)/CoA‐free and Phosphate‐balanced In Vitro Synthetic Enzymatic Biosystem

Enzyme‐Catalysed Synthesis of Secondary and Tertiary Amides

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