dc.contributor.author	Fehlau, Maryke
dc.contributor.author	Kaspar, Felix
dc.contributor.author	Hellendahl, Katja F.
dc.contributor.author	Schollmeyer, Julia
dc.contributor.author	Neubauer, Peter
dc.contributor.author	Wagner, Anke
dc.date.accessioned	2020-10-29T14:30:57Z
dc.date.available	2020-10-29T14:30:57Z
dc.date.issued	2020-08-06
dc.date.updated	2020-10-26T10:06:36Z
dc.description	A correction to this article has been published in Front. Bioeng. Biotechnol., 26 October 2020 \| https://doi.org/10.3389/fbioe.2020.606584	en
dc.description	Eine Korrektur zu diesem Artikel wurde publiziert in Front. Bioeng. Biotechnol., 26 October 2020 \| https://doi.org/10.3389/fbioe.2020.606584	de
dc.description.abstract	Nucleoside-5’-triphosphates (NTPs) and their analogs are building blocks of DNA and are important compounds in both pharmaceutical and molecular biology applications. Currently, commercially available base or sugar modified NTPs are mainly synthesized chemically. Since the chemical production of NTPs is time-consuming and generally inefficient, alternative approaches are under development. Here we present a simple, efficient and generalizable enzymatic synthesis method for the conversion of nucleosides to NTPs. Our one-pot method is modular, applicable to a wide range of natural and modified nucleotide products and accesses NTPs directly from cheap nucleoside precursors. Nucleoside kinases, nucleoside monophosphate (NMP) kinases and a nucleoside diphosphate (NDP) kinase were applied as biocatalysts. Enzymes with different substrate specificities were combined to produce derivatives of adenosine and cytidine triphosphate with conversions of 4 to 26%. The implementation of a (deoxy)ATP recycling system resulted in a significant increase in the conversion to all NTP products, furnishing 4 different NTPs in quantitative conversion. Natural (deoxy)NTPs were synthesized with 60 to >99% conversion and sugar- and base-modified NTPs were produced with 69 to >99% and 27 to 75% conversion, respectively. The presented method is suitable for the efficient synthesis of a wide range of natural and modified NTPs in a sustainable one-pot process.	en
dc.description.sponsorship	TU Berlin, Open-Access-Mittel – 2020	en
dc.description.sponsorship	DFG, 392246628, Chemo-enzymatische Synthese von Selen-modifizierten Nukleosiden, Nukleotiden und Oligonukleotiden	en
dc.identifier.eissn	2296-4185
dc.identifier.uri	https://depositonce.tu-berlin.de/handle/11303/11802
dc.identifier.uri	http://dx.doi.org/10.14279/depositonce-10691
dc.language.iso	en	en
dc.relation.ispartof	10.14279/depositonce-18262
dc.relation.issupplementedby	10.3389/fbioe.2020.606584
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/	en
dc.subject.ddc	570 Biowissenschaften; Biologie	de
dc.subject.other	enzymatic cascade synthesis	en
dc.subject.other	nucleoside-5′-triphosphate	en
dc.subject.other	one-pot multi-enzyme reaction	en
dc.subject.other	nucleotide analog	en
dc.subject.other	nucleotide kinase	en
dc.subject.other	nucleoside kinase	en
dc.subject.other	modular	en
dc.subject.other	ATP regeneration system	en
dc.title	Modular Enzymatic Cascade Synthesis of Nucleotides Using a (d)ATP Regeneration System	en
dc.type	Article	en
dc.type.version	publishedVersion	en
dcterms.bibliographicCitation.articlenumber	854	en
dcterms.bibliographicCitation.doi	10.3389/fbioe.2020.00854	en
dcterms.bibliographicCitation.journaltitle	Frontiers in Bioengineering and Biotechnology	en
dcterms.bibliographicCitation.originalpublishername	Frontiers	en
dcterms.bibliographicCitation.originalpublisherplace	Lausanne	en
dcterms.bibliographicCitation.volume	8	en
tub.accessrights.dnb	free	en
tub.affiliation	Fak. 3 Prozesswissenschaften::Inst. Biotechnologie::FG Bioverfahrenstechnik	de
tub.affiliation.faculty	Fak. 3 Prozesswissenschaften	de
tub.affiliation.group	FG Bioverfahrenstechnik	de
tub.affiliation.institute	Inst. Biotechnologie	de
tub.publisher.universityorinstitution	Technische Universität Berlin	en

Modular Enzymatic Cascade Synthesis of Nucleotides Using a (d)ATP Regeneration System

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